KR20130059404A - 원핵생물 발현 구축물 - Google Patents
원핵생물 발현 구축물 Download PDFInfo
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Abstract
본 발명은 원핵생물 세포에서 관심 폴리펩타이드의 발현에 유용한 프로-폴리펩타이드를 보고한다. 따라서, 상기 프로-폴리펩타이드를 상기 관심 폴리펩타이드의 N-말단에 융합시킨다. 본 발명에 보고된 바와 같은 상기 프로-폴리펩타이드는 개선된 발현 수율을 제공하고 상기 융합 폴리펩타이드의 취급(하류 가공과정, 정제)을 개선시킨다. 예를 들어, 상기 프로-폴리펩타이드를 포함하는 관심 단백질이 예를 들어 친화성 크로마토그래피 물질에 결합되어 있는 동안 효율적인 내독소 제거가 수행된다. 그 후에, 상기 프로-폴리펩타이드는 동족 프로테아제를 갖는 통합된 프로테아제 절단 부위에 의해 상기 관심 폴리펩타이드로부터 효율적으로 절단될 수 있다.
Description
본 발명은 원핵생물 세포에서 폴리펩타이드의 생산을 위한 발현 구축물을 보고한다. 상기 발현 구축물은 N-에서 C-말단 방향으로 다이펩타이드 GS, 아미노산 태그, 다이펩타이드 GS 및 프로테아제 절단 부위를 포함하는 프로-폴리펩타이드를 포함한다.
재조합 폴리펩타이드의 생산을 위한 발현 시스템들은 현재의 발달 상태로 널리 공지되어 있으며 예를 들어 문헌[Marino, M.H., Biopharm. 2 (1989) 18-33]; [Goeddel, D.V., et al., Methods Enzymol. 185 (1990) 3-7]; [Wurm, F., and Bernard, A., Curr. Opin. Biotechnol. 10 (1999) 156-159]에 개시되어 있다.
약학적 용도에 사용하기 위한 폴리펩타이드, 예를 들어 항체 및 항체 융합물은 일반적으로 CHO 세포, NS0 세포, SP2/0 세포, COS 세포, HEK 세포, BHK 세포, PER.C6(등록상표) 세포 등과 같은 포유동물 세포에서 일반적으로 생산된다. 진핵생물 발현 플라스미드의 요소는 일반적으로, 에스케리키아 콜라이의 경우, 원핵생물 복제 기원 및 원핵생물 선택 마커, 진핵생물 선택 마커, 및 관심 구조 유전자(들)(각각의 유전자는 프로모터, 구조 유전자 및 폴리아데닐화 신호를 포함하는 전사 종결자를 포함한다)의 발현을 위한 하나 이상의 발현 카세트를 포함하는 원핵생물 플라스미드 번식 단위이다. 포유동물 세포에서 일시적인 발현을 위해서, 포유동물 복제 기원, 예를 들어 SV40 Ori 또는 OriP를 포함시킬 수 있다. 프로모터로서 구성 또는 유도성 프로모터가 선택될 수 있다. 최적화된 전사를 위해서 코작(Kozak) 서열을 5' 번역되지 않은 영역에 포함시킬 수도 있다. mRNA 가공과정, 특히 mRNA 스플라이싱 및 전사 종결의 경우, 구조 유전자의 조직(엑손/인트론 조직)에 따라, mRNA 스플라이싱 신호뿐만 아니라 폴리아데닐화 신호를 포함시킬 수도 있다.
약학적 용도에 사용하기 위한 다른 폴리펩타이드, 예를 들이 인슐린, 인터페론 알파-2, 소마토트로핀, 인터류킨-2, GM-CSF 및 레테플라제는 원핵생물 세포, 효모 및 주로 에스케리키아 콜라이에서 생산될 수 있다. 에스케리키아 콜라이 발현 플라스미드의 요소는 일반적으로 복제 기원, 선택 마커, 및 관심 구조 유전자(들)의 발현을 위한 하나 이상의 발현 카세트이다. 발현 카세트는 일반적으로 프로모터, 구조 유전자, 및 전사 종결자를 포함한다. 프로모터로서 구성 또는 유도성 프로모터를 사용할 수 있다. 최적화된 전사를 위해서 mRNA의 개시 코돈에 선행하는 샤인-달가르노-서열(Shine-Dalgarno-Sequence) 또는 그의 변체를 5' 번역되지 않은 영역에 포함시킬 수도 있다.
본 발명은 원핵생물 세포에서 관심 폴리펩타이드의 발현에 유용한 프로-폴리펩타이드를 보고한다. 따라서, 상기 프로-폴리펩타이드를 상기 관심 폴리펩타이드의 N-말단에 융합시킨다. 본 발명에 보고된 바와 같은 상기 프로-폴리펩타이드는 개선된 발현 수율을 제공하고 상기 융합 폴리펩타이드의 취급(하류 가공과정, 정제)을 개선시킨다. 예를 들어, 상기 프로-폴리펩타이드를 포함하는 관심 단백질이 예를 들어 친화성 크로마토그래피 물질에 결합되어 있는 동안 효율적인 내독소 제거가 수행된다. 그 후에, 상기 프로-폴리펩타이드는 동족 프로테아제를 갖는 통합된 프로테아제 절단 부위에 의해 상기 관심 폴리펩타이드로부터 효율적으로 절단될 수 있다.
본 발명에서 하나의 태양으로서 N-에서 C-말단 방향으로
-아미노산 서열 GS를 갖는 제 1 다이펩타이드,
-아미노산 서열 태그,
-효소 절단 부위에 바로 인접하여 아미노산 서열 GS를 갖는 제 2 다이펩타이드,
-상기 효소 절단 부위
를 포함하는 프로-폴리펩타이드를 보고한다.
하나의 실시태양에서, 상기 프로-폴리펩타이드는 상기 아미노산 서열 GS를 갖는 제 1 다이펩타이드에 대해 N-말단에 선도 아미노산 서열을 포함한다. 또 다른 태양에서, 상기 선도 아미노산 서열은 2 개 이상 20 개 이하의 아미노산 잔기의 길이를 갖는다. 추가의 실시태양에서 상기 선도 아미노산 서열은 2 개 이상 10 개 이하의 아미노산 잔기의 길이를 갖는다. 또한 하나의 실시태양에서 상기 선도 아미노산 서열은 서열번호 1 내지 8 중에서 선택된 아미노산 서열을 갖는 폴리펩타이드이다. 추가의 실시태양에서 상기 선도 아미노산 서열은 서열번호 1 내지 6 중에서 선택된 아미노산 서열을 갖는 폴리펩타이드이다.
하나의 실시태양에서 상기 프로-폴리펩타이드는 N-에서 C-말단 방향으로
-선도 아미노산 서열,
-아미노산 서열 GS를 갖는 제 1 다이펩타이드,
-아미노산 서열 태그,
-효소 절단 부위에 바로 인접하여 아미노산 서열 GS를 갖는 제 2 다이펩타이드
-상기 효소 절단 부위
로 이루어진다.
본 발명에 보고된 바와 같은 추가의 태양은 N-에서 C-말단 방향으로
-임의로 선도 아미노산 서열,
-아미노산 서열 GS를 갖는 제 1 다이펩타이드,
-아미노산 서열 태그,
-효소 절단 부위에 바로 인접하여 아미노산 서열 GS를 갖는 제 2 다이펩타이드,
-상기 효소 절단 부위, 및
-관심 단백질
을 포함하는 융합 폴리펩타이드이다.
앞서 보고된 바와 같은 모든 태양의 하나의 실시태양에서 상기 아미노산 서열 태그는 서열번호 9 내지 서열번호 27 중에서 선택된 아미노산 서열을 갖는다. 하나의 실시태양에서 상기 아미노산 서열 태그는 서열번호 11 또는 서열번호 15의 아미노산 서열을 갖는다. 또 다른 실시태양에서 상기 효소 절단 부위는 서열번호 28 내지 서열번호 42 중에서 선택된 아미노산 서열을 갖는다. 추가의 실시태양에서 상기 관심 폴리펩타이드는 항체 중쇄 또는 경쇄, 항체 단편, 단쇄 항체, 아포지방단백질, 아포지방단백질 변체, 아포지방단백질 융합물, 인터페론, 인터류킨, 인슐린, 조직 유형 플라스미노겐 활성화제 변체, 콜로니-자극 인자, 성장 호르몬, 골 형태발생 단백질 중에서 선택된다. 하나의 실시태양에서 상기 관심 폴리펩타이드는 서열번호 43 또는 서열번호 44 또는 서열번호 45의 아미노산 서열을 갖는다. 하나의 실시태양에서 상기 관심 폴리펩타이드는 본 발명에 보고된 바와 같은 프로-폴리펩타이드와 상이한 폴리펩타이드이다, 즉 상기 관심 폴리펩타이드는 아미노산 서열 태그에 직접 융합된 아미노산 서열 GS를 갖는 다이펩타이드에 상응하는 아미노산 서열을 포함하지 않는다. 하나의 실시태양에서 상기 관심 폴리펩타이드의 N-말단의 아미노산은 하류 가공과정 후에 유리 알파-아미노 기를 갖는다. 하나의 실시태양에서 상기 프로-폴리펩타이드 및/또는 관심 폴리펩타이드는 글리코실화되지 않는다.
본 발명에서 또 다른 태양으로서 하기의 단계를 포함하는 관심 폴리펩타이드의 제조 방법을 보고한다
(a) N-에서 C-말단 방향으로
-임의로 선도 아미노산 서열,
-아미노산 서열 GS를 갖는 제 1 다이펩타이드,
-아미노산 서열 태그,
-효소 절단 부위에 바로 인접하여 아미노산 서열 GS를 갖는 제 2 다이펩타이드
-상기 효소 절단 부위, 및
-관심 단백질
을 포함하는 융합 폴리펩타이드를 암호화하는 핵산을 포함하는 세포를 제공하는 단계,
(b) 상기 세포를 배양하는 단계,
(c) 상기 세포 또는 배양 배지로부터 상기 융합 폴리펩타이드를 회수하는 단계,
(d) 상기 융합 폴리펩타이드를 정제하는 단계,
(e) 상기 융합 폴리펩타이드를 효소에 의해 절단하는 단계에 의해 관심 폴리펩타이드를 생성시킨다.
하나의 실시태양에서 상기 세포는 원핵생물 세포이다. 또 다른 실시태양에서 상기 세포는 에스케리키아 콜라이 또는 바실러스 서브틸리스 세포이다. 하나의 실시태양에서 상기 아미노산 서열 태그는 서열번호 9 내지 서열번호 27 중에서 선택된 아미노산 서열을 갖는다. 하나의 실시태양에서 상기 아미노산 서열 태그는 서열번호 11 또는 서열번호 15의 아미노산 서열을 갖는다. 또 다른 실시태양에서 상기 효소 절단 부위는 서열번호 28 내지 서열번호 42 중에서 선택된 아미노산 서열을 갖는다. 또한 하나의 실시태양에서 상기 추가의 폴리펩타이드는 항체 중쇄 또는 경쇄, 항체 단편, 단쇄 항체, 아포지방단백질, 아포지방단백질 변체, 아포지방단백질 융합물, 인터페론, 인터류킨, 인슐린, 조직 유형 플라스미노겐 활성화제 변체, 콜로니-자극 인자, 성장 호르몬, 골 형태발생 단백질 중에서 선택된다. 하나의 실시태양에서 상기 관심 폴리펩타이드는 서열번호 43 또는 서열번호 44 또는 서열번호 45의 아미노산 서열을 갖는다. 하나의 실시태양에서 상기 관심 폴리펩타이드는 본 발명에 보고된 바와 같은 프로-폴리펩타이드와 상이한 폴리펩타이드이다, 즉 상기 추가의 폴리펩타이드는 아미노산 서열 태그에 직접 융합된 아미노산 서열 GS를 갖는 다이펩타이드를 포함하지 않는다.
본 발명에서 추가의 태양으로서 5'-에서 3'-방향으로
-아미노산 서열 GS를 갖는 다이펩타이드를 암호화하는 핵산,
-아미노산 서열 태그를 암호화하는 핵산,
-효소 절단 부위를 암호화하는 핵산에 바로 인접하여 아미노산 서열 GS를 갖는 다이펩타이드를 암호화하는 핵산,
-상기 효소 절단 부위를 암호화하는 핵산
을 포함하는 핵산을 포함하는 부분들의 키트를 보고한다.
본 발명에 보고된 바와 같은 하나의 태양은
-원핵생물 세포를 글루코스, 효모 추출물, L-류신, L-프롤린, L-메티오닌, 티아민-HCl, 소포제를 포함하는 배지에서 배양하고,
-상기 세포에 효모 추출물, 글리세롤, L-메티오닌, L-류신 및 L-프롤린을 포함하는 제 1 공급물 용액을 공급하고,
-상기 세포에 L-프롤린을 포함하는 제 2 공급물 용액을 공급하고,
-수산화 칼륨 용액 및 글루코스 용액을 pH 조절에 사용함
을 특징으로 하는, 상기 원핵생물 세포의 배양 방법이다.
본 발명에 보고된 바와 같은 하나의 태양은
-폴리펩타이드를 암호화하는 핵산을 포함하는 세포를 글루코스, 효모 추출물, L-류신, L-프롤린, L-메티오닌, 티아민-HCl, 소포제를 포함하는 배지에서 배양하고,
-상기 세포에 효모 추출물, 글리세롤, L-메티오닌, L-류신 및 L-프롤린을 포함하는 제 1 공급물 용액을 공급하고,
-상기 세포에 L-프롤린을 포함하는 제 2 공급물 용액을 공급하고,
-수산화 칼륨 용액 및 글루코스 용액을 pH 조절에 사용함
을 특징으로 하고, 상기 폴리펩타이드를 상기 세포 또는 상기 배양 배지로부터 회수하고 이에 의해 폴리펩타이드를 생성시키는, 상기 폴리펩타이드의 제조 방법이다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 제 1 공급물의 첨가를 578 ㎚에서 측정된 약 15의 광학 밀도에서 출발하고, 상기 제 2 공급물의 첨가를 578 ㎚에서 측정된 약 50의 광학 밀도에서 출발하고, 상기 폴리펩타이드의 발현을 578 ㎚에서 측정된 약 90의 광학 밀도에서 IPTG로 유도한다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 배지는 약 8.85 g/ℓ의 글루코스, 약 63.5 g/ℓ의 효모 추출물, 약 2.2 g/ℓ의 NH4Cl, 약 1.95 g/ℓ의 L-류신, 약 2.9 g/ℓ의 L-프롤린, 약 0.75 g/ℓ의 L-메티오닌, 약 17.3 g/ℓ의 KH2PO4*3H2O, 약 2 g/ℓ의 MgSO4*7H2O, 약 25.8 ㎎/ℓ의 티아민-HCl, 약 1.0 ㎖/ℓ의 10% 소포제를 포함한다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 제 1 공급물 용액은 약 333 g/ℓ의 효모 추출물, 약 333 g/ℓ의 85% 글리세롤, 약 1.7 g/ℓ의 L-메티오닌, 및 약 5 g/ℓ의 L-류신 및 L-프롤린 각각을 포함한다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 제 2 공급물 용액은 약 600 g/ℓ의 L-프롤린을 포함한다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 pH 조절용 염기는 10%(w/v) KOH 용액이고 상기 산은 75% 글루코스 용액이다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 배양은 약 25 ℃에서이다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 배양은 약 pH 6.5 내지 약 pH 6.9의 pH에서이다.
하나의 실시태양에서 상기 배양은 약 10 ℓ의 부피에서이다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 제 1 공급물을 70 g/h의 비율로 출발한다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 제 2 공급물을 10 ㎖/h의 비율로 출발한다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 용존 산소 값을 50% 이상으로 유지시킨다. 특정한 실시태양에서, 상기 용존 산소 값을, 교반기 속도, 통기율, 및 공기압을 동시에 증가시킴으로써 50% 이상으로 유지시킨다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 교반기 속도는 약 500 rpm 내지 약 1500 rpm이다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 통기율은 약 10 ℓ/분 내지 약 20 ℓ/분이다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 공기압은 약 300 mbar 내지 약 500 mbar이다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 원핵생물 세포는 에스케리키아 콜라이 세포이다.
본 발명에 보고된 바와 같은 방법의 하나의 실시태양에서, 상기 폴리펩타이드는 아포지방단백질 A1이다. 구체적인 실시태양에서 상기 아포지방단백질 A1은 테트라넥틴-아포지방단백질 A1 전구체 단백질이다.
본 발명에 보고된 바와 같은 하나의 태양은 약 8.85 g/ℓ의 글루코스, 약 63.5 g/ℓ의 효모 추출물, 약 2.2 g/ℓ의 NH4Cl, 약 1.95 g/ℓ의 L-류신, 약 2.9 g/ℓ의 L-프롤린, 약 0.75 g/ℓ의 L-메티오닌, 약 17.3 g/ℓ의 KH2PO4*3H2O, 약 2 g/ℓ의 MgSO4*7H2O, 약 25.8 ㎎/ℓ의 티아민-HCl, 약 1.0 ㎖/ℓ의 10% 소포제를 포함하는 원핵생물 세포용 배양 배지이다.
하나의 실시태양에서, 상기 배지는 약 333 g/ℓ의 효모 추출물, 약 333 g/ℓ의 85% 글리세롤, 약 1.7 g/ℓ의 L-메티오닌, 및 약 5 g/ℓ의 L-류신 및 L-프롤린 각각을 포함하는 제 1 공급물을 추가로 포함한다.
하나의 실시태양에서, 상기 배지는 약 600 g/ℓ의 L-프롤린을 포함하는 제 2 공급물 용액을 추가로 포함한다.
본 발명에 보고된 프로-폴리펩타이드는 원핵생물 세포에서 관심 폴리펩타이드의 발현에 유용하다. 상기 프로-폴리펩타이드는 개선된 발현 수율을 제공하고 취급, 예를 들어 하류 가공과정 및 정제를 개선시킨다. 예를 들어, 상기 프로-폴리펩타이드를 포함하는 관심 단백질이 예를 들어 친화성 크로마토그래피 물질에 결합되어 있는 동안 효율적인 내독소 제거가 수행된다. 그 후에, 상기 프로-폴리펩타이드는 동족 프로테아제를 갖는 통합된 프로테아제 절단 부위에 의해 상기 관심 폴리펩타이드로부터 효율적으로 절단될 수 있다.
본 발명에서 N-에서 C-말단 방향으로
-임의로 선도 아미노산 서열,
-제 1 다이펩타이드 GS,
-아미노산 서열 태그,
-효소 절단 부위에 바로 인접한 제 2 다이펩타이드 GS
-상기 효소 절단 부위
를 포함하는 프로-폴리펩타이드를 보고한다.
본 출원 내에서 사용된 바와 같은 "아미노산" 또는 "아미노산 잔기"란 용어는 직접 또는 전구체의 형태로 핵산에 의해 암호화될 수 있는 카복시 α-아미노산의 기를 나타낸다. 개별적인 아미노산은 3 개의 뉴클레오타이드, 소위 코돈 또는 3 개 염기로 이루어지는 핵산에 의해 암호화된다. 각각의 아미노산은 하나 이상의 코돈에 의해 암호화된다. 이는 "유전 암호의 축퇴"로서 공지되어 있다. 본 출원 내에서 사용된 바와 같은 "아미노산"이란 용어는 알라닌(3 글자 암호: ala, 1 글자 암호: A), 아르기닌(arg, R), 아스파라진(asn, N), 아스파트산(asp, D), 시스테인(cys, C), 글루타민(gln, Q), 글루탐산(glu, E), 글리신(gly, G), 히스티딘(his, H), 아이소류신(ile, I), 류신(leu, L), 리신(lys, K), 메티오닌(met, M), 페닐알라닌(phe, F), 프롤린(pro, P), 세린(ser, S), 쓰레오닌(thr, T), 트립토판(trp, W), 타이로신(tyr, Y), 및 발린(val, L)을 포함하는 천연 카복시 α-아미노산을 나타낸다.
"폴리펩타이드"란 용어는 천연으로 생성되었든지 합성으로 생성되었든지 간에, 펩타이드 결합에 의해 결합된 아미노산들로 이루어지는 중합체를 나타낸다. 약 20 개 미만 아미노산 잔기의 폴리펩타이드를 "펩타이드"라 칭할 수 있는 반면, 2 개 이상의 폴리펩타이드로 이루어지거나 또는 100 개 초과 아미노산 잔기의 하나의 폴리펩타이드를 포함하는 분자는 "단백질"이라 칭할 수 있다. "다이펩타이드"란 용어는 펩타이드 결합에 의해 서로 연결된 2 개의 아미노산 잔기로 이루어지는 펩타이드를 나타낸다. 폴리펩타이드는 또한 비-아미노산 성분, 예를 들어 탄수화물 그룹, 금속 이온, 또는 카복실산 에스터를 포함할 수도 있다. 상기 비-아미노산 성분은, 상기 폴리펩타이드가 발현되는 세포에 의해 첨가될 수도 있으며, 세포의 유형에 따라 변할 수 있다. 폴리펩타이드를 본 발명에서는 그의 아미노산 주쇄 구조 또는 이를 암호화하는 핵산에 의해 정의한다. 탄수화물 그룹과 같은 첨가는 일반적으로 자세히 명시하지 않지만, 그럼에도 불구하고 존재할 수도 있다. 하나의 실시태양에서 관심 폴리펩타이드는 아포지방단백질 또는 아포지방단백질 변체/융합물이다. 또 다른 실시태양에서 상기 아포지방단백질은 아포지방단백질 A1 또는 아포지방단백질 A1 변체/융합물이다. 추가의 실시태양에서 상기 아포지방단백질 A1은 테트라넥틴 삼량체화 도메인에 N-말단 융합되어 인공 테트라넥틴-아포지방단백질 A1 융합 폴리펩타이드를 생성시킨다. 하나의 실시태양에서 상기 관심 폴리펩타이드는 서열번호 43 내지 서열번호 76 중에서 선택된 아미노산 서열을 갖는다. 또 다른 실시태양에서 상기 관심 폴리펩타이드는 서열번호 43 및 서열번호 44 및 서열번호 45 중에서 선택된 아미노산 서열을 갖는다.
"선도 아미노산 서열"이란 용어는 펩타이드 결합을 통해 서로 연결된 아미노산들 또는 아미노산 잔기들의 서열을 나타낸다. 하나의 실시태양에서 상기 선도 아미노산 서열은 1 내지 20 개의 아미노산 잔기로 이루어진다. 또 다른 실시태양에서 상기 선도 아미노산 서열은 2 내지 15 개의 아미노산 잔기로 이루어진다. 추가의 실시태양에서 상기 선도 아미노산 서열은 4 내지 10 개의 아미노산 잔기로 이루어진다. 또한 하나의 실시태양에서 상기 선도 아미노산 서열은 MR, 또는 서열번호 1(KAKRFKKH), 또는 서열번호 2(AHFWQQA), 또는 서열번호 3(CDLPQTHSL), 또는 서열번호 4(IEPD), 또는 서열번호 5(IEPDSPGT), 또는 서열번호 6(MCDLPQTHSL), 또는 서열번호 7(AEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGAEARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS), 또는 서열번호 8(TDPEFQQQQQLDVVKRQQELLRLTVWGTKNLQARVTAIEKYLQDQARLNSWGCAFRQVCHTTVPWVNDSLAPDWDNMTWQEWEKQVRYLEANISKSLEQAQIQQEKNMYELQKLNSWDIRSVV)의 아미노산 서열을 갖는다. 추가의 실시태양에서 상기 선도 아미노산 서열은 MR, 및 서열번호 1(KAKRFKKH), 및 서열번호 2(AHFWQQA), 및 서열번호 3(CDLPQTHSL), 및 서열번호 4(IEPD), 및 서열번호 5(IEPDSPGT), 및 서열번호 6(MCDLPQTHSL) 중에서 선택된 아미노산 서열을 갖는다.
"아미노산 서열 태그"란 용어는 특이적인 결합 성질을 갖는 펩타이드 결합을 통해 서로 연결된 아미노산 잔기들의 서열을 나타낸다. 하나의 실시태양에서 상기 아미노산 서열 태그는 친화성 또는 정제 태그이다. 하나의 실시태양에서 상기 아미노산 서열 태그는 Arg-태그, His-태그, 플래그(Flag)-태그, 3x플래그-태그, 스트렙(Strep)-태그, 나노-태그, SBP-태그, c-myc-태그, S-태그, 칼모듈린-결합-펩타이드, 셀룰로스-결합-도메인, 키틴-결합-도메인, GST-태그, 및 MBP-태그 중에서 선택된다. 추가의 실시태양에서 상기 아미노산 서열 태그는 서열번호 9(RRRRR) 및 서열번호 10(RRRRRR), 및 서열번호 11(HHHHHH), 및 서열번호 12(KDHLIHNVHKEFHAHAHNK) 및 서열번호 13(DYKDDDDK) 및 서열번호 14(DYKDHDGDYKDHDIDYKDDDDK) 및 서열번호 15(AWRHPQFGG) 및 서열번호 16(WSHPQFEK) 및 서열번호 17(MDVEAWLGAR) 및 서열번호 18(MDVEAWLGARVPLVET) 및 서열번호 19(MDEKTTGWRGGHVVEGLAGELEQLRARLEHHPQGQREP) 및 서열번호 20(EQKLISEEDL) 및 서열번호 21(KETAAAKFERQHMDS) 및 서열번호 22(KRRWKKNFIAVSAANRFKKISSSGAL) 및 서열번호 23(셀룰로스 결합 도메인) 및 서열번호 24(셀룰로스 결합 도메인) 및 서열번호 25(TNPGVSAWQVNTAYTAGQLVTYNGKTYKCLQPHTSLAGWEP SNVPALWQLQ) 및 서열번호 26(GST-태그) 및 서열번호 27(MBP-태그) 중에서 선택된다.
"효소 절단 부위"란 용어는 프로테아제에 의해 특이적으로 절단될 수 있는 펩타이드 결합을 통해 서로 연결된 아미노산 잔기들의 서열을 나타낸다. 하나의 실시태양에서 상기 프로테아제는 IgA-프로테아제, 그랜자임(Granzyme) B, Tev프로테아제, 예비절단(Prescission) 프로테아제, 트롬빈, 인자 Xa, 또는 엔테로키나제이다.
"IgA-프로테아제"란 용어는 하기의 서열들 중 하나를 포함하는 인식 부위를 갖는 네이세리아 고노로에아에(Neisseria gonorrhoeae)로부터 유도된 프로테아제를 나타내며, 여기에서 "↓"는 절단된 결합의 위치를 나타낸다.
Pro-Ala-Pro ↓ Ser-Pro (서열번호 28),
Pro-Pro ↓ Ser-Pro (서열번호 29),
Pro-Pro ↓ Ala-Pro (서열번호 30),
Pro-Pro ↓ Thr-Pro (서열번호 31),
Pro-Pro ↓ Gly-Pro (서열번호 32),
Pro-Arg-Pro-Pro ↓ Thr-Pro (서열번호 33),
Val-Val-Ala-Pro-Pro ↓ Ala-Pro (서열번호 34),
Val-Val-Ala-Pro-Pro ↓ Ser-Pro (서열번호 35),
Val-Val-Ala-Pro-Pro ↓ Thr-Pro (서열번호 36),
Val-Val-Ala-Pro-Pro ↓ Gly-Pro (서열번호 37),
Ala-Pro-Pro-Ala ↓ Ala-Pro (서열번호 39),
Pro-Arg-Pro-Pro ↓ Ala-Pro (서열번호 40),
Pro-Arg-Pro-Pro ↓Ser-Pro (서열번호 41),
Pro-Arg-Pro-Pro ↓Gly-Pro (서열번호 42).
"작동적으로 결합된"이란 용어는 2 개 이상 성분들의 병치를 나타내며, 여기에서 상기와 같이 개시된 성분들은 상기 성분들이 그들이 의도하는 방식으로 작용하도록 하는 관계로 놓인다. 예를 들어, 분비 리더 및 폴리펩타이드와 같은 2 개의 폴리펩타이드 암호화 영역들을 결합시키는 관계로 놓인다.
핵산을 암호화하는 아미노산 서열의 결합은 당해 분야에 공지된 재조합 방법에 의해, 예를 들어 PCR 방법을 사용하고/하거나 편리한 제한 부위에서의 연결에 의해 수행된다. 편리한 제한 부위가 존재하지 않는 경우, 합성 올리고뉴클레오타이드 어댑터 또는 링커를 통상적인 관행에 따라 사용한다.
특히 원핵생물 세포에서 관심 폴리펩타이드의 재조합 생산을 위해 높은 발현 수율 및 실행 가능한 하류 처리과정이 고려된다.
본 발명에 보고된 바와 같이 N-에서 C-말단 방향으로
-제 1 다이펩타이드 GS,
-아미노산 서열 태그,
-제 2 다이펩타이드 GS, 및
-효소 절단 부위
를 포함하는 프로-폴리펩타이드는 작동적으로 결합된 관심 폴리펩타이드의 발현에 유용하다. 유리한 성질들은 본 발명에 보고된 바와 같은 프로-폴리펩타이드가, 원핵생물 세포에서 재조합 수단에 의해 발현되도록 되어 있는 관심 폴리펩타이드의 N-말단에 융합될 때 발휘될 수 있다. 따라서, 본 발명에 보고된 바와 같은 프로-폴리펩타이드를 발현 효율 및 하류 가공과정의 개선에 사용할 수 있다. 상기 관심 폴리펩타이드는 본 발명에 보고된 바와 같은 프로-폴리펩타이드 및 상기 관심 폴리펩타이드를 포함하는 융합 폴리펩타이드로서 원핵생물 세포에 의해 발현된다. 즉 상기 융합 폴리펩타이드는 N-에서 C-말단 방향으로 본 발명에 보고된 바와 같은 프로-폴리펩타이드 및 상기 관심 폴리펩타이드를 포함한다.
상이한 융합 폴리펩타이드들의 발현 수율. 각 세포에 제공된 첫 번째 수율 값을 실시예 3b에 따른 발효 방법에 의해 수득하였으며, 각 세포에서 두 번째 수율 값은 실시예 3a에 따른 발효 방법에 의해 수득하였다. | ||||||||
융합 폴리펩타이드의 N-말단 프로- 폴리펩타이드의 요소들 |
융합
폴리펩타
이드의 분자량
[g/ mol ] |
수율
[g/ℓ] |
수율
[10 -3 mol /ℓ] |
|||||
선도 아미노산 서열 | 다이펩타이드 | 아미노산 서열 태그 | 다이펩타이드 | 중재 아미노산 서열 | 효소 절단 부위 | |||
MR | GS | HHHHHH | GS | n.p. | PRPPTP | 34904.1 | 24.312.8 | 0.696 0.367 |
MCDLPQTHSL | GS | HHHHHH | GS | n.p. | VVAPPAP | 35472.7 | 20.310.5 | 0.572 0.296 |
MR | GS | HHHHHH | GS | AEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGAEARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS | VVAPPAP | 48373.5 | 7.9 3.5 |
0.163 0.072 |
MR | GS | HHHHHH | n.p. | AHFWQQA | PRPPTP | 35372.5 | 9.0 2.4 |
0.254 0.068 |
MR | GS | HHHHHH | n.p. | TDPEFQQQQQLLDVVKRQQELLRLTVWGTKNLQARVTAIEKYLQDQARLNSWGCAFRQVCHTTVPWVNDSLAPDWDNMTWQEWEKQVRYLEANISKSLEQAQIQQEKNMYELQKLNSWDIRSVV | APPAAP | 49653.5 | 10.27.0 | 0.205 0.141 |
M | n.p. | HHHHHH | n.p. | KAKRFKKH | PRPPAP | 35453.9 | 11.12.6 | 0.313 0.073 |
n.p. = 존재하지 않음 |
표 1로부터, N-말단에서 제 2 다이펩타이드 GS와 효소 절단 부위 사이에 추가의 아미노산 서열이 삽입되지 않은 본 발명에 보고된 바와 같은 프로-폴리펩타이드를 포함하는 융합 폴리펩타이드는 중재 아미노산 서열을 포함하는 것들보다 더 높은 발현 수율을 제공하는 것을 알 수 있다. 2 개 이상의 아미노산 잔기의 선도 아미노산 서열이 상기 제 1 다이펩타이드 GS에 대해 N-말단에 존재할 수도 있다.
본 발명에 보고된 바와 같은 프로-폴리펩타이드는 그의 C-말단에 효소 절단 부위를 함유한다. 상기 효소 절단 부위는 프로테아제에 대한 인식 동기를 함유하는 아미노산 서열이다. 상기 인식 부위는 상기 프로테아제가 상기 인식 부위에서 특이적으로 절단하는 한, 즉 상기 서열이 상기 융합 폴리펩타이드의 전체 아미노산 서열 중 오직 한 번만 존재하는 한, 임의의 프로테아제에 대한 것일 수 있다.
상기 융합 폴리펩타이드가 친화성 크로마토그래피 물질에, 즉 상기 관심 폴리펩타이드에 대해서 특이적으로 설계된 것이 아니라 아미노산 서열 태그에 대해서 설계된 친화성 물질에 결합된 동안 내독소 제거가 가능한 것이 특히 유리하다. 이러한 결합 성질에 의해서 아미노산 서열 태그와 상응하는 친화성 물질의 임의의 상응하는 조합을 사용할 수 있다. 상기 내독소 제거 후에 상기 관심 폴리펩타이드를 프로테아제 절단 부위를 사용함으로써 상기 융합 폴리펩타이드로부터 효율적으로 제거할 수 있다.
하기의 실시예 및 서열 목록을 본 발명의 이해를 돕기 위해 제공하고, 본 발명의 진정한 범위는 첨부된 특허청구범위에 나타낸다. 본 발명의 진의로부터 이탈됨 없이 나타낸 과정들에 변경을 수행할 수 있는 것으로 생각된다.
서열 목록에 대한 설명
서열번호 1 내지 8 아미노산 서열
서열번호 9 내지 27 아미노산 태그
서열번호 28 내지 42 프로테아제 절단 부위
서열번호 43 내지 76 아포지방단백질 아미노산 서열
서열번호 77 내지 78 변형 아포지방단백질 융합 아미노산 서열
서열번호 79 내지 84 프로-폴리펩타이드 아미노산 서열
실시예
물질 및 방법
재조합
DNA
기법
문헌[Sambrook, J., et al., Molecular Cloning: A Laboratory Manual; Cold Spring Harbor Laboratory Press, 2nd edition, New York, (December 1989)]에 개시된 바와 같이 표준 방법을 사용하여 DNA를 조작하였다. 분자 생물학 시약들을 제조자의 설명에 따라 사용하였다.
유전자 합성
목적하는 유전자 구획을 화학 합성에 의해 제조된 올리고뉴클레오타이드로부터 제조하였다. 단일의 제한 엔도뉴클레아제 절단 효소가 측면에 인접한 상기 유전자 구획들을, PCR 증폭을 포함하는 올리고뉴클레오타이드의 어닐링 및 연결에 의해 조립하고 후속으로 A-돌출부를 통해 pCR2.1-TOPO-TA 클로닝 벡터(인비트로젠 코포레이션(Invitrogen Corp.), 미국 소재) 내로 클로닝하였다. 상기 서브클로닝된 유전자 단편들의 DNA 서열을 DNA 서열화에 의해 확인하였다.
실시예
1
에스케리키아 콜라이 발현 플라스미드의 제조 및 설명
테트라넥틴-아포지방단백질 A1 융합 폴리펩타이드를 재조합 수단에 의해 제조하였다. 3 개의 상이한 테트라넥틴-아포지방단백질 A1 융합 폴리펩타이드의 아미노산 서열을 하기에 제공한다(굵은 선, 테트라넥틴-삼량체화 도메인, 변체 A 및 B). 변체 A는 변체 B와, 상기 테트라넥틴 도메인의 N-말단에서 2 개의 아미노산 잔기의 첨가에 의해 상이하다. 변체 C는 변체 A와, 상기 테트라넥틴 도메인의 C-말단 단부에서 5 개의 아미노산 잔기의 첨가에 의해 상이하다.
변체 A의 아미노산 서열(서열번호 44):
1 IVNAKKDVVN TKMFEELKSR LDTLAQEVAL LKEQQALQTV DEPPQSPWDR
51 VKDLATVYVD VLKDSGRDYV SQFEGSALGK QLNLKLLDNW DSVTSTFSKL
101 REQLGPVTQE FWDNLEKETE GLRQEMSKDL EEVKAKVQPY LDDFQKKWQE
151 EMELYRQKVE PLRAELQEGA RQKLHELQEK LSPLGEEMRD RARAHVDALR
201 THLAPYSDEL RQRLAARLEA LKENGGARLA EYHAKATEHL STLSEKAKPA
251 LEDLRQGLLP VLESFKVSFL SALEEYTKKL NTQ
변체 B의 아미노산 서열(서열번호 77):
1 KKIVNAKKD VVNTKMFEEL KSRLDTLAQE VALLKEQQAL QTVDEPPQSP
51 WDRVKDLATV YVDVLKDSGR DYVSQFEGSA LGKQLNLKLL DNWDSVTSTF
101 SKLREQLGPV TQEFWDNLEK ETEGLRQEMS KDLEEVKAKV QPYLDDFQKK
151 WQEEMELYRQ KVEPLRAELQ EGARQKLHEL QEKLSPLGEE MRDRARAHVD
201 ALRTHLAPYS DELRQRLAAR LEALKENGGA RLAEYHAKAT EHLSTLSEKA
251 KPALEDLRQG LLPVLESFKV SFLSALEEYT KKLNTQ
변체 C의 아미노산 서열(서열번호 78):
1 IVNAKKDVVN TKMFEELKSR LDTLAQEVAL LKEQQALQTV SLKGTDEPPQ
51 SPWDRVKDLA TVYVDVLKDS GRDYVSQFEG SALGKQLNLK LLDNWDSVTS
101 TFSKLREQLG PVTQEFWDNL EKETEGLRQE MSKDLEEVKA KVQPYLDDFQ
151 KKWQEEMELY RQKVEPLRAE LQEGARQKLH ELQEKLSPLG EEMRDRARAH
201 VDALRTHLAP YSDELRQRLA ARLEALKENG GARLAEYHAK ATEHLSTLSE
251 KAKPALEDLR QGLLPVLESF KVSFLSALEE YTKKLNTQ
상기 테트라넥틴-아포지방단백질 A1 융합 폴리펩타이드는 에스케리키아 콜라이에서 전구체 폴리펩타이드(더 큰 융합 폴리펩타이드)로서 발현되었다. 하기의 N-말단 프로-폴리펩타이드를 개선된 발현 수율 및 하류 가공과정에 대해 시험하였다:
1)
변체
B와
결합된
프로-
폴리펩타이드(플라스미드 5803)의
아미노산 서열:
MRGSHHHHHH GSPRPPTP (서열번호 79)
프로-폴리펩타이드 5803은 N-에서 C-말단 방향으로
-아미노산 서열 MR을 갖는 선도 아미노산 서열,
-제 1 다이펩타이드 GS,
-HHHHHH(서열번호 11)의 아미노산 서열을 갖는 헥사-히스티딘 태그,
-제 2 다이펩타이드 GS, 및
-PRPPTP(서열번호 33)의 아미노산 서열을 갖는 IgA 프로테아제 절단 부위
를 포함하는 인공 폴리펩타이드이다.
2)
변체
A와
결합된
프로-
폴리펩타이드(플라스미드 5816)의
아미노산 서열:
MCDLPQTHSL GSHHHHHHGS VVAPPAP (서열번호 80)
프로-폴리펩타이드 5816은 N-에서 C-말단 방향으로
-MCDLPQTHSL(서열번호 3)의 아미노산 서열을 갖는 인터페론 서열의 단편에 접합된 메티오닌을 암호화하는 선도 아미노산 서열,
-제 1 다이펩타이드 GS,
-HHHHHH(서열번호 11)의 아미노산 서열을 갖는 헥사-히스티딘 태그,
-제 2 다이펩타이드 GS, 및
-VVAPPAP(서열번호 32)의 아미노산 서열을 갖는 IgA 프로테아제 절단 부위
를 포함하는 인공 폴리펩타이드이다.
3)
변체
A와
결합된
프로-
폴리펩타이드(플라스미드 5820)의
아미노산 서열:
1 MRGSHHHHHH GSAEAGITGT WYNQLGSTFI VTAGADGALT GTYESAVGNA
51 ESRYVLTGRY DSAPATDGSG TALGWTVAWK NNYRNAHSAT TWSGQYVGGA
101 EARINTQWLL TSGTTEANAW KSTLVGHDTF TKVKPSAASV VAPPAP
(서열번호 81)
프로-폴리펩타이드 5820은 N-에서 C-말단 방향으로
-아미노산 서열 MR을 갖는 선도 아미노산 서열,
-제 1 다이펩타이드 GS,
-HHHHHH(서열번호 11)의 아미노산 서열을 갖는 헥사-히스티딘 태그,
-제 2 다이펩타이드 GS,
-스트렙트아비딘으로부터 유도된 중재 아미노산 서열, 및
-VVAPPAP(서열번호 34)의 아미노산 서열을 갖는 IgA 프로테아제 절단 부위
를 포함하는 인공 폴리펩타이드이다.
4)
변체
A와
결합된
프로-
폴리펩타이드(플라스미드 5805)의
아미노산 서열:
MRGSHHHHHH AHFWQQAPRP PTP (서열번호 82)
프로-폴리펩타이드 5805는 N-에서 C-말단 방향으로
-아미노산 서열 MR을 갖는 선도 아미노산 서열,
-제 1 다이펩타이드 GS,
-HHHHHH(서열번호 11)의 아미노산 서열을 갖는 헥사-히스티딘 태그,
-아미노산 서열 AHFWQQA(서열번호 2)를 갖는 중재 아미노산 서열, 및
-PRPPTP(서열번호 38)의 아미노산 서열을 갖는 IgA 프로테아제 절단 부위
를 포함하는 인공 폴리펩타이드이다.
5)
변체
C와
결합된
프로-
폴리펩타이드(플라스미드 5819)의
아미노산 서열:
1 MRGSHHHHHH TDPEFQQQQQ LLDVVKRQQE LLRLTVWGTK NLQARVTAIE
51 KYLQDQARLN SWGCAFRQVC HTTVPWVNDS LAPDWDNMTW QEWEKQVRYL
101 EANISKSLEQ AQIQQEKNMY ELQKLNSWDI RSVVAPPAP
(서열번호 83)
프로-폴리펩타이드 5819는 N-에서 C-말단 방향으로
-아미노산 서열 MR을 갖는 선도 아미노산 서열,
-제 1 다이펩타이드 GS,
-HHHHHH(서열번호 11)의 아미노산 서열을 갖는 헥사-히스티딘 태그,
-인간 HIV2 gp32 단백질로부터 유도된 중재 아미노산 서열, 및
-VVAPPAP(서열번호 34)의 아미노산 서열을 갖는 IgA 프로테아제 절단 부위
를 포함하는 인공 폴리펩타이드이다.
6)
변체
B와
결합된
프로-
폴리펩타이드(플라스미드 5806)의
아미노산 서열:
MHHHHHHKAK RFKKHPRPPAP (서열번호 84)
프로-폴리펩타이드 5806은 N-에서 C-말단 방향으로
-선도 아미노산 서열(M, 개시 코돈),
-HHHHHH(서열번호 11)의 아미노산 서열을 갖는 헥사-히스티딘 태그,
-KAKRFKKH(서열번호 1)의 아미노산 서열을 갖는 중재 아미노산 서열, 및
-PRPPAP(서열번호 40)의 아미노산 서열을 갖는 IgA 프로테아제 절단 부위
를 포함하는 인공 폴리펩타이드이다.
상기 테트라넥틴-아포지방단백질 A1 변체 폴리펩타이드를 IgA 프로테아제를 사용하여 시험관 내에서 효소 절단에 의해 상기 융합 전구체 단백질로부터 회수하였다.
5803, 5816, 5820, 5805, 5819 및 5806으로 표시된, 상이한 프로-폴리펩타이드 테트라넥틴-아포지방단백질 A1 암호화 융합 유전자를 적합한 핵산 구획의 연결에 의해 공지된 재조합 방법 및 기법으로 조립하였다. 핵산 서열을 화학 합성에 의해 제조하였으며 DNA 서열화에 의해 확인하였다.
기본/개시 에스케리키아
콜라이
발현 플라스미드 4980의 제조 및 설명
플라스미드 4980(4980-pBRori-URA3-LACI-SAC)은 에스케리키아 콜라이에서 코어-스트렙트아비딘의 발현을 위한 발현 플라스미드이다. 상기 플라스미드는 435 bp 길이의 코어-스트렙트아비딘 암호화 EcoRI/CelII-단편을 갖는 플라스미드 1966(1966-pBRori-URA3-LACI-T-반복부; EP-B 1 422 237에 보고되어 있다)으로부터 유도된 3142 bp 길이의 EcoRI/CelII-단편의 연결에 의해 생성되었다.
상기 코어-스트렙트아비딘 에스케리키아 콜라이 발현 플라스미드는 하기의 요소들을 포함한다:
-에스케리키아 콜라이에서 복제를 위한 벡터 pBR322로부터의 복제 기원(문헌[Sutcliffe, J.G., et al., Quant. Biol. 43 (1979) 77-90]에 따른 bp 위치 2517-3160에 상응함),
-에스케리키아 콜라이 pyrF 돌연변이체 균주(유라실 영양요구성)의 상보성에 의한 플라스미드 선택을 허용하는 오로티딘 5'-포스페이트 데카복실라제를 암호화하는 사카로마이세스 세레비지아에의 URA3 유전자(문헌[Rose, M., et al., Gene 29 (1984) 113-124]),
-하기로 형성된 코어-스트렙트아비딘 발현 카세트
문헌[Stuber, D. et al.](이전 참조)에 따른 합성 리보솜 결합 부위를 포함하는 T5 하이브리드 프로모터(문헌[Bujard, H., et al., Methods. Enzymol. 155 (1987) 416-433] 및 [Stueber, D., et al., Immunol. Methods IV (1990) 121-152]에 따른 T5-PN25/03/04 하이브리드 프로모터),
코어-스트렙트아비딘 유전자, 및
2 개의 박테리오파지-유도된 전사 종결자, λ-T0 종결자(문헌[Schwarz, E., et al., Nature 272 (1978) 410-414]), 및 fd-종결자(문헌[Beck, E., and Zink, B., Gene 1-3 (1981) 35-58]), 및
-에스케리키아 콜라이로부터의 lacI 억제 유전자(문헌[Farabaugh, P.J., Nature 274 (1978) 765-769]).
프로-
폴리펩타이드를
포함하는 최종 발현 플라스미드(플라스미드 5803, 5816, 5820, 5805, 5819 및 5806)의 제조
플라스미드 5803(5803-His6-IgA-TP7-TripB-ApoAI)은 프로-폴리펩타이드 5803을 함유하는 테트라넥틴-아포지방단백질 A1 전구체 단백질의 발현을 위한 플라스미드이다. 상기 플라스미드는, 단일의 측면 인접 EcoRI 및 CelII 제한 엔도뉴클레아제 절단 부위를 사용하여 벡터 4980으로부터 코어-스트렙트아비딘 구조 유전자를 절제하고 958 bp 길이의 EcoRII/CelII 5803 프로-폴리펩타이드 테트라넥틴-아포지방단백질 A1 전구체 단백질 암호화 유전자 구획을 3142 bp 길이의 EcoRI/CelII-4980 벡터 단편에 삽입하여 제조되었다.
플라스미드
5816 (5816-IFN-His6-IgA-API10-TripB-ApoAI),
5820 (5820-His6-coreSA-IgA-API10-TripB-ApoA1),
5805 (5805-His6-IgA-Pro-TPI10-TripB-ApoAI),
5819 (5819-gp32-His6-IgA-API10-TriB-SLKGT-ApoA1), 및
5806 (5806-His6-IgA-Opt-AP7-TripB-ApoAI)
를 이전에 플라스미드 5803에 대해 개시한 바와 같이 생성시켰다.
실시예
2
에스케리키아 콜라이에서 플라스미드 5803, 5816, 5820, 5805, 5819 및 5806으로부터 테트라넥틴-아포지방단백질 A1 전구체 단백질의 발현
테트라넥틴-아포지방단백질 A1 전구체 단백질 5803, 5816, 5820, 5805, 5819 및 5806의 발현을 위해서, 에스케리키아 콜라이 영양요구성(PyrF)의 상보성에 의한 무-항생제 플라스미드를 선택할 수 있게 하는 에스케리키아 콜라이 숙주/벡터 시스템을 사용하였다(예를 들어 EP-B 0 972 838 및 미국 특허 제 6,291,245 호를 참조하시오).
상기 테트라넥틴-아포지방단백질 A1 전구체 단백질을 에스케리키아 콜라이 균주 CSPZ-2(leuB, proC, trpE, thi-1, ΔpyrF)에서 발현시켰다.
선택성 배지에서
pyrF
영양요구성의
상보성에 의한 형질전환 및 세포 배양
에스케리키아 콜라이 K12 균주 CSPZ-2(leuB, proC, trpE, thi-1, ΔpyrF)를 선행 단계에서 수득한 발현 플라스미드들(각각 5803, 5816, 5820, 5805, 5819 및 5806)로 형질전환시켰다. 상기 형질전환된 CSPZ-2 세포를 먼저 37 ℃에서 아가 플레이트 상에서 증식시키고 후속으로 0.5% 카사미노산(디프코(Difco))을 함유하는 M9 최소 배지에서 진탕 배양물 중에서 550 ㎚에서 0.6 내지 0.9의 광학 밀도까지 증식시키고 후속으로 IPTG(1 내지 5 mmol/ℓ 최종 농도)로 유도하였다.
37 ℃에서 4 내지 16 시간의 유도 기간 후에, 상기 세포질 및 용해성의 발현된 테트라넥틴-아포지방단백질 A1 전구체 단백질은, 삼각 플라스크 중의 전체 배양물 브로쓰를 수확 전에 1 내지 2 시간 동안 50 ℃로 가열하는 가열 단계에 의해, 불용성 단백질 응집체, 소위 봉입체로 전이되었다. 그 후에, 상기 세포를 원심분리에 의해 수확하고, 50 mmol/ℓ의 칼륨 포스페이트 완충제, pH 6.5로 세척하고, 추가의 가공과정까지 -20 ℃에서 보관하였다.
발현 분석
발현 분석을 위해서 원심분리된 배양 배지의 3 개의 OD550 ㎚ 단위(1 OD550 ㎚ = 550 ㎚에서 1의 OD를 갖는 1 ㎖의 세포 현탁액)로부터 세포 펠릿을 0.25 ㎖의 10 mmol/ℓ 칼륨 포스페이트 완충제, pH 6.5에 재현탁하고, 상기 세포를 초음파 처리(50% 강도에서 30 초의 2 회 펄스)에 의해 용해시켰다. 상기 불용성 세포 성분들이 침전되었으며(원심분리 14,000 rpm, 5 분) 상등액을 그의 1/5 부피의 5xSDS 샘플 완충제(1xSDS 샘플 완충제: 50 mmol/ℓ 트리스-HCl, pH6.8, 1% SDS, 50 mmol/ℓ DTT, 10% 글리세롤, 0.001% 브로모페놀 블루)와 혼합하였다. 상기 불용성 세포 찌꺼기 분획(펠릿)을 0.3 ㎖의 1xSDS 샘플 완충제에 재현탁하고, 상기 샘플을 95 ℃에서 5 분간 배양하고 다시 원심분리시켰다. 후속으로, 상기 단백질을 SDS 폴리아크릴아미드 젤 전기영동(PAGE)(문헌[Laemmli, U.K., Nature 227 (1970) 680-685])에 의해 분리시키고 쿠마씨 브릴리언트 블루(Coomassie Brilliant Blue) R 염료로 염색하였다.
상기 합성된 테트라넥틴-아포지방단백질 A1 전구체 단백질은 균질하였으며 불용성 단백질 응집체(IB)의 형태로 불용성 세포 찌꺼기 분획 중에서 발견되었다. 상기 발현 수율은 모든 클론들에서 측정 정확도의 범위 내에서 필적할만하였으며 전체 에스케리키아 콜라이 단백질에 대해 30 내지 60%였다.
실시예
3
테트라넥틴-아포지방단백질 A1 전구체 단백질의 재조합 생산을 위한 에스케리키아 콜라이의 10 ℓ 고 세포 밀도 발효
실시예
3a
예비-배양
예비-배양을 위해서 약 1 g/ℓ의 L-류신, 약 1 g/ℓ의 L-프롤린 및 약 1 ㎎/ℓ의 티아민-HCl이 보충된 문헌[Sambrook, J., et al., Molecular Cloning: A Laboratory Manual; Cold Spring Harbor Laboratory Press; 2nd edition, New York, (December 1989)]에 따른 M9 배지를 사용하였다.
예비-배양을 위해서 배플을 갖는 1000 ㎖ 삼각-플라스크 중의 M9-배지 300 ㎖에 1차 시드 뱅크 앰풀 2 ㎖을 접종하였다. 상기 배양을 1 내지 3의 광학 밀도(578 ㎚)가 획득될 때까지 37 ℃에서 13 시간 동안 회전 진탕기 상에서 수행하였다.
10 ℓ 유가(
fed
-
batch
) 주 발효
발효를 위해서 문헌[Riesenberg, et al.]에 따른 배치 배지를 사용하였다(문헌[Riesenberg, D., et al., J. Biotechnol. 20 (1991) 17-27]: 27.6 g/ℓ 글루코스*H2O, 13.3 g/ℓ KH2PO4, 4.0 g/ℓ (NH4)2HPO4, 1.7 g/ℓ 시트레이트, 1.2 g/ℓ MgSO4*7 H2O, 60 mg/ℓ 철(III) 시트레이트, 2.5 mg/ℓ CoCl2*6 H2O, 15 mg/ℓ MnCl2*4 H2O, 1.5 mg/ℓ CuCl2*2 H2O, 3 mg/ℓ H3BO3, 2.5 mg/ℓ Na2MoO4*2 H2O, 8 mg/ℓ Zn(CH3COO)2*2 H2O, 8.4 mg/ℓ 티트리플렉스(Titriplex) III, 1.3 ml/ℓ 신페로닉(Synperonic) 10% 소포제). 상기 배치 배지에 5.4 ㎎/ℓ 티아민-HCl 및 1.2 g/ℓ L-류신 및 L-프롤린 각각을 보충하였다. 공급물 1 용액은 19.7 g/ℓ MgSO4*7H2O가 보충된 700 g/ℓ 글루코스를 함유하였다. pH 조절용 알칼리 용액은 50 g/ℓ L-류신 및 50 g/ℓ L-프롤린이 각각 보충된 수성 12.5%(w/v) NH3 용액이었다.
상기 발효를 10 ℓ 바이오스탯(Biostat) C DCU3 발효기(자르토리우스(Sartorius) 독일 멜슝겐 소재)에서 수행하였다. 6.4 ℓ 멸균 발효 배치 배지 + 상기 예비-배양으로부터의 300 ㎖의 접종물로 출발하여, 배치 발효를 37 ℃, pH 6.9±0.2, 500 mbar에서 10 ℓ/분의 통기율로 수행하였다. 처음에 보충된 글루코스가 고갈된 후에, 온도를 28 ℃로 이동시켰으며 상기 발효가 유가 방식에 돌입하였다. 여기에서 용존 산소(pO2)의 상대적인 값을, 공급물 1을 일정하게 증가하는 교반기 속도(10 시간 이내에 550 rpm으로부터 1000 rpm까지 및 16 시간 이내에 1000 rpm으로부터 1400 rpm까지) 및 통기율(10 시간 동안 10 ℓ/분으로부터 16 ℓ/분까지 및 5 시간 동안 16 ℓ/분으로부터 20 ℓ/분까지)와 함께 첨가함으로써 50%로 유지시켰다(DO-염, 예를 들어 문헌[Shay, L.K., et al., J. Indus. Microbiol. (1987) 79-85]을 참조하시오). 상기 추가적인 아미노산과의 공급은 상기 알칼리 용액의 첨가로부터 생성되었으며, 이때 pH는 대략 8 시간의 배양 후에 조절 하한(6.70)에 도달하였다. 상기 재조합 치료 단백질의 발현은 70의 광학 밀도에서 1 mM IPTG의 첨가에 의해 유도되었다.
바이오매스
수확
상기 발효의 끝에서 세포질성 및 용해성의 발현된 테트라넥틴-아포지방단백질 A1은, 상기 발효기 중의 전체 배양물 브로쓰를 수확 전에 1 내지 2 시간 동안 50 ℃로 가열하는 가열 단계에 의해, 불용성 단백질 응집체, 소위 봉입체로 전이된다(예를 들어 EP-B 1 486 571을 참조하시오). 그 후에, 상기 발효기의 내용물을 병류 원심분리기로 원심분리시키고(13,000 rpm, 13 ℓ/h), 수확된 바이오매스를 추가의 가공과정까지 -20 ℃에서 보관하였다. 상기 합성된 테트라넥틴-아포지방단백질 A1 전구체 단백질은 불용성 단백질 응집체, 소위 봉입체(IB)의 형태로 오직 불용성 세포 찌꺼기 분획에서만 독점적으로 발견되었다.
생성물 정량분석
상기 발효기로부터 취한 샘플들(하나는 유도 전의 것이고 다른 것들은 단백질 발현 유도 후 전용 시점에서의 것들)을 SDS-폴리아크릴아미드 젤 전기영동으로 분석한다. 모든 샘플로부터 동일한 양의 세포(OD표적 = 5)를 5 ㎖의 PBS 완충제에 현탁하고 얼음 상에서 초음파 처리를 통해 분쇄시켰다. 이어서 100 ㎕의 각 현탁액을 원심분리하고(15,000 rpm, 5 분), 각 상등액을 회수하고 별도의 바이알로 옮긴다. 이는 용해성과 불용성의 발현된 표적 단백질을 구별하기 위한 것이다. 각 상등액(=용해성) 분획에 300 ㎕, 및 각 펠릿(=불용성) 분획에 400 ㎕의 SDS 샘플 완충제(문헌[Laemmli, U.K., Nature 227 (1970) 680-685])를 가한다. 샘플들을 진탕 하에 95 ℃에서 15 분간 가열하여 상기 샘플들 중의 모든 단백질들을 용해시키고 환원시켰다. 실온으로 냉각시킨 후에 5 ㎕의 각 샘플을 4 내지 20% TGX 기준 염색 부재 폴리아크릴아미드 젤(바이오-래드(Bio-Rad))로 옮긴다. 추가로 5 ㎕의 분자량 표준(프리시즌 플러스 프로테인 스탠다드(Precision Plus Protein Standard, 바이오-래드) 및 기지의 생성물 단백질 농도(0.1 ㎍/㎕)를 갖는 3 개 량(0.3 ㎕, 0.6 ㎕ 및 0.9 ㎕)의 정량분석 기준을 상기 젤 상에 위치시킨다.
상기 전기영동을 200 V에서 60 분간 실행시켰으며 그 후에 상기 젤을 GelDOC EZ 이미저(바이오-래드)로 옮기고 UV 조사 하에 5 분간 처리하였다. 젤 상들을 이미지 랩(Image Lab) 분석 소프트웨어(바이오-래드)를 사용하여 분석하였다. 상기 3 개 표준을 사용하여 >0.99의 계수로 선형 회귀 곡선을 계산하고 이로부터 원래 샘플 중의 표적 단백질의 농도를 계산하였다.
실시예
3b
예비-배양
예비-배양을 위해서 약 1 g/ℓ의 L-류신, 약 1 g/ℓ의 L-프롤린 및 약 1 ㎎/ℓ의 티아민-HCl이 보충된 문헌[Sambrook, J., et al., Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press; 2nd edition, New York, (December 1989)]에 따른 M9 배지를 사용하였다.
예비-배양을 위해서 배플을 갖는 1000 ㎖ 삼각-플라스크 중의 변형된 M9-배지 300 ㎖에 아가 플레이트로부터, 또는 1차 시드 뱅크 앰풀 1 내지 2 ㎖을 접종하였다. 상기 배양을 1 내지 3의 광학 밀도(578 ㎚)가 획득될 때까지 37 ℃에서 13 시간 동안 회전 진탕기 상에서 수행하였다.
10 ℓ 유가 주 발효
발효 및 테트라넥틴-아포지방단백질 A1의 고 수율 발현을 위해서 하기의 배치 배지 및 공급물들을 사용하였다:
8.85 g/ℓ 글루코스, 63.5 g/ℓ 효모 추출물, 2.2 g/ℓ NH4Cl, 1.94 g/ℓ L-류신, 2.91 g/ℓ L-프롤린, 0.74 g/ℓ L-메티오닌, 17.3 g/ℓ KH2PO4*H2O, 2.02 g/ℓ MgSO4*7H2O, 25.8 mg/ℓ 티아민-HCl, 1.0 ml/ℓ 신페로닉 10% 소포제. 상기 공급물 1 용액은 1.67 g/ℓ L-메티오닌 및 5 g/ℓ L-류신 및 L-프롤린 각각이 보충된 333 g/ℓ 효모 추출물 및 333 g/ℓ 85% 글리세롤을 함유하였다. 상기 공급물 2는 600 g/ℓ L-프롤린의 용액이었다. 상기 pH 조절용 알칼리 용액은 10%(w/v) KOH 용액이었으며 산으로서 75% 글루코스 용액을 사용하였다. 모든 성분들은 탈이온수에 용해되었다.
상기 발효를 10 ℓ 바이오스탯 C DCU3 발효기(자르토리우스, 독일 멜슝겐 소재)에서 수행하였다. 5.15 ℓ 멸균 발효 배치 배지 + 상기 예비-배양으로부터의 300 ㎖의 접종물로 출발하여, 유가 발효를 25 ℃, pH 6.7±0.2, 300 mbar에서 10 ℓ/분의 통기율로 수행하였다. 처음에 보충된 글루코스가 고갈되기 전에, 상기 배양물은 15의 광학 밀도(578 ㎚)에 도달하였으며 상기 발효가 유가 방식에 돌입하였고 이때 공급물 1을 70 g/h로 출발하였다. 상기 배양물 중의 글루코스 농도를 모니터하면서 공급물 1을, 글루코스 축적을 피하고 pH를 6.9의 조절 상한 부근으로 유지시키면서 최대 150 g/ℓ로 증가시켰다. 50의 광학 밀도(578 ㎚)에서, 공급물 2는 10 ㎖/h의 일정한 공급률로 시작하였다. 용존 산소(pO2)의 상대적인 값을, 교반기 속도(500 rpm에서 1500 rpm), 통기율(10 ℓ/분으로부터 20 ℓ/분까지) 및 압력(300 mbar로부터 500 mbar까지)을 동시에 증가시킴으로써 50% 이상으로 유지시켰다. 상기 재조합 치료 단백질의 발현은 90의 광학 밀도에서 1 mM IPTG의 첨가에 의해 유도되었다.
생성물 정량분석
상기 발효기로부터 취한 7 개의 샘플들(하나는 유도 전의 것이고 다른 것들은 단백질 발현 유도 후 전용 시점에서의 것들)을 SDS-폴리아크릴아미드 젤 전기영동으로 분석한다. 모든 샘플로부터 동일한 양의 세포(OD표적 = 5)를 5 ㎖의 PBS 완충제에 현탁하고 얼음 상에서 초음파 처리를 통해 분쇄시켰다. 이어서 100 ㎕의 각 현탁액을 원심분리하고(15,000 rpm, 5 분), 각 상등액을 회수하고 별도의 바이알로 옮긴다. 이는 용해성과 불용성의 발현된 표적 단백질을 구별하기 위한 것이다. 각 상등액(=용해성) 분획에 300 ㎕, 및 각 펠릿(=불용성) 분획에 200 ㎕의 SDS 샘플 완충제(문헌[Laemmli, U.K., Nature 227 (1970) 680-685])를 가한다. 샘플들을 진탕 하에 95 ℃에서 15 분간 가열하여 상기 샘플들 중의 모든 단백질들을 용해시키고 환원시켰다. 실온으로 냉각시킨 후에 5 ㎕의 각 샘플을 10% 비스-트리스 폴리아크릴아미드 젤(노바겐(Novagen))로 옮긴다. 추가로 5 ㎕의 분자량 표준(프리시즌 플러스 프로테인 스탠다드, 바이오-래드) 및 기지의 생성물 단백질 농도(0.1 ㎍/㎕)를 갖는 3 개 량(0.3 ㎕, 0.6 ㎕ 및 0.9 ㎕)의 정량분석 기준을 상기 젤 상에 위치시킨다.
상기 전기영동을 200 V에서 35 분간 실행시켰으며 이어서 상기 젤을 쿠마씨 브릴리언트 블루 R 염료로 염색하고, 가열된 물로 탈염시키고, 디지털화를 위해서 광학 농도계(GS710, 바이오-래드)로 옮겼다. 젤 상들을 콴터티 원(Quantity One) 1-D 분석 소프트웨어(바이오-래드)를 사용하여 분석하였다. 상기 3 개 표준을 사용하여 >0.98의 계수로 선형 회귀 곡선을 계산하고 이로부터 원래 샘플 중의 표적 단백질의 농도를 계산하였다.
바이오매스
수확
상기 발효의 끝에서 세포질성 및 용해성의 발현된 테트라넥틴-아포지방단백질 A1은, 상기 발효기 중의 전체 배양물 브로쓰를 수확 전에 1 내지 2 시간 동안 50 ℃로 가열하는 가열 단계에 의해, 불용성 단백질 응집체, 소위 봉입체(IB)로 전이되었다(예를 들어 EP-B 1 486 571 참조하시오). 상기 가열 단계 후에, 상기 합성된 테트라넥틴-아포지방단백질 A1 전구체 단백질은 IB의 형태로 오직 불용성 세포 찌꺼기 분획에서만 독점적으로 발견되었다.
상기 발효기의 내용물을 4 내지 8 ℃로 냉각시키고, 병류 원심분리기로 원심분리시키고(13,000 rpm, 13 ℓ/h), 수확된 바이오매스를 추가의 가공과정까지 -20 ℃에서 보관한다. 상기 수확된 총 바이오매스 수율은 상기 발현된 구축물에 따라 건조 물질 39 g/ℓ 내지 90 g/ℓ의 범위였다.
SEQUENCE LISTING
<110> F. Hoffmann-La Roche AG
<120> Prokaryotic expression construct
<130> 26973
<140> PCT/EP2011/064599
<141> 2011-08-25
<150> EP10008996.0
<151> 2010-08-30
<150> EP10187663.9
<151> 2010-10-15
<160> 84
<170> PatentIn version 3.5
<210> 1
<211> 8
<212> PRT
<213> Artificial Sequence
<220>
<223> short amino acid sequence
<400> 1
Lys Ala Lys Arg Phe Lys Lys His
1 5
<210> 2
<211> 7
<212> PRT
<213> Artificial Sequence
<220>
<223> short amino acid sequence
<400> 2
Ala His Phe Trp Gln Gln Ala
1 5
<210> 3
<211> 9
<212> PRT
<213> Artificial Sequence
<220>
<223> short amino acid sequence
<400> 3
Cys Asp Leu Pro Gln Thr His Ser Leu
1 5
<210> 4
<211> 4
<212> PRT
<213> Artificial Sequence
<220>
<223> short amino acid sequence
<400> 4
Ile Glu Pro Asp
1
<210> 5
<211> 8
<212> PRT
<213> Artificial Sequence
<220>
<223> short amino acid sequence
<400> 5
Ile Glu Pro Asp Ser Pro Gly Thr
1 5
<210> 6
<211> 10
<212> PRT
<213> Artificial Sequence
<220>
<223> short amino acid sequence
<400> 6
Met Cys Asp Leu Pro Gln Thr His Ser Leu
1 5 10
<210> 7
<211> 127
<212> PRT
<213> Artificial Sequence
<220>
<223> short amino acid sequence
<400> 7
Ala Glu Ala Gly Ile Thr Gly Thr Trp Tyr Asn Gln Leu Gly Ser Thr
1 5 10 15
Phe Ile Val Thr Ala Gly Ala Asp Gly Ala Leu Thr Gly Thr Tyr Glu
20 25 30
Ser Ala Val Gly Asn Ala Glu Ser Arg Tyr Val Leu Thr Gly Arg Tyr
35 40 45
Asp Ser Ala Pro Ala Thr Asp Gly Ser Gly Thr Ala Leu Gly Trp Thr
50 55 60
Val Ala Trp Lys Asn Asn Tyr Arg Asn Ala His Ser Ala Thr Thr Trp
65 70 75 80
Ser Gly Gln Tyr Val Gly Gly Ala Glu Ala Arg Ile Asn Thr Gln Trp
85 90 95
Leu Leu Thr Ser Gly Thr Thr Glu Ala Asn Ala Trp Lys Ser Thr Leu
100 105 110
Val Gly His Asp Thr Phe Thr Lys Val Lys Pro Ser Ala Ala Ser
115 120 125
<210> 8
<211> 124
<212> PRT
<213> Artificial Sequence
<220>
<223> short amino acid sequence
<400> 8
Thr Asp Pro Glu Phe Gln Gln Gln Gln Gln Leu Leu Asp Val Val Lys
1 5 10 15
Arg Gln Gln Glu Leu Leu Arg Leu Thr Val Trp Gly Thr Lys Asn Leu
20 25 30
Gln Ala Arg Val Thr Ala Ile Glu Lys Tyr Leu Gln Asp Gln Ala Arg
35 40 45
Leu Asn Ser Trp Gly Cys Ala Phe Arg Gln Val Cys His Thr Thr Val
50 55 60
Pro Trp Val Asn Asp Ser Leu Ala Pro Asp Trp Asp Asn Met Thr Trp
65 70 75 80
Gln Glu Trp Glu Lys Gln Val Arg Tyr Leu Glu Ala Asn Ile Ser Lys
85 90 95
Ser Leu Glu Gln Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu
100 105 110
Gln Lys Leu Asn Ser Trp Asp Ile Arg Ser Val Val
115 120
<210> 9
<211> 5
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 9
Arg Arg Arg Arg Arg
1 5
<210> 10
<211> 6
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 10
Arg Arg Arg Arg Arg Arg
1 5
<210> 11
<211> 6
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 11
His His His His His His
1 5
<210> 12
<211> 19
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 12
Lys Asp His Leu Ile His Asn Val His Lys Glu Phe His Ala His Ala
1 5 10 15
His Asn Lys
<210> 13
<211> 8
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 13
Asp Tyr Lys Asp Asp Asp Asp Lys
1 5
<210> 14
<211> 22
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 14
Asp Tyr Lys Asp His Asp Gly Asp Tyr Lys Asp His Asp Ile Asp Tyr
1 5 10 15
Lys Asp Asp Asp Asp Lys
20
<210> 15
<211> 9
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag#
<400> 15
Ala Trp Arg His Pro Gln Phe Gly Gly
1 5
<210> 16
<211> 8
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 16
Trp Ser His Pro Gln Phe Glu Lys
1 5
<210> 17
<211> 10
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 17
Met Asp Val Glu Ala Trp Leu Gly Ala Arg
1 5 10
<210> 18
<211> 16
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 18
Met Asp Val Glu Ala Trp Leu Gly Ala Arg Val Pro Leu Val Glu Thr
1 5 10 15
<210> 19
<211> 38
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 19
Met Asp Glu Lys Thr Thr Gly Trp Arg Gly Gly His Val Val Glu Gly
1 5 10 15
Leu Ala Gly Glu Leu Glu Gln Leu Arg Ala Arg Leu Glu His His Pro
20 25 30
Gln Gly Gln Arg Glu Pro
35
<210> 20
<211> 10
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 20
Glu Gln Lys Leu Ile Ser Glu Glu Asp Leu
1 5 10
<210> 21
<211> 15
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 21
Lys Glu Thr Ala Ala Ala Lys Phe Glu Arg Gln His Met Asp Ser
1 5 10 15
<210> 22
<211> 26
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 22
Lys Arg Arg Trp Lys Lys Asn Phe Ile Ala Val Ser Ala Ala Asn Arg
1 5 10 15
Phe Lys Lys Ile Ser Ser Ser Gly Ala Leu
20 25
<210> 23
<211> 47
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 23
Pro Ala Thr Thr Thr Gly Ser Ser Pro Gly Pro Thr Gln Ser His Tyr
1 5 10 15
Gly Gln Cys Gly Gly Ile Gly Tyr Ser Gly Pro Thr Val Cys Ala Ser
20 25 30
Gly Thr Thr Cys Gln Val Leu Asn Pro Tyr Tyr Ser Gln Cys Leu
35 40 45
<210> 24
<211> 32
<212> PRT
<213> Butyrivibrio fibrisolvens
<400> 24
Met Asp Trp Asn Ala Asn Ile Ala Pro Gly Asn Ser Val Glu Phe Gly
1 5 10 15
Ile Gln Gly Ala Gly Ser Val Gly Asn Val Ile Asp Ile Thr Val Glu
20 25 30
<210> 25
<211> 51
<212> PRT
<213> Artificial Sequence
<220>
<223> amino acid tag
<400> 25
Thr Asn Pro Gly Val Ser Ala Trp Gln Val Asn Thr Ala Tyr Thr Ala
1 5 10 15
Gly Gln Leu Val Thr Tyr Asn Gly Lys Thr Tyr Lys Cys Leu Gln Pro
20 25 30
His Thr Ser Leu Ala Gly Trp Glu Pro Ser Asn Val Pro Ala Leu Trp
35 40 45
Gln Leu Gln
50
<210> 26
<211> 209
<212> PRT
<213> Chondrus crispus
<400> 26
Met Pro Glu Ile Lys Leu Thr Tyr Phe Asp Met Arg Gly Arg Ala Glu
1 5 10 15
Ala Ser Arg Leu Ala Leu Val Val Gly Glu Ile Pro Phe Glu Asp Glu
20 25 30
Arg Val Val Phe Asp His Trp Lys Glu Ala Lys Pro Lys Thr Pro Tyr
35 40 45
Ala Ala Leu Pro Met Leu Thr Val Asp Gly Met Gln Val Ala Gln Ser
50 55 60
Asp Ala Ile Leu Arg Tyr Cys Gly Lys Leu Ala Gly Leu Tyr Pro Ser
65 70 75 80
Asp Pro Leu Glu Ala Ala Lys Val Asp Glu Val Gly Gly Val Ile Asp
85 90 95
Asp Val Thr His Ala Met Tyr Arg Tyr Arg Gly Asp Asp Lys Asp Lys
100 105 110
Leu Arg Glu Glu Arg Asp Lys Phe Ser Lys Val Asp Val Pro Arg Tyr
115 120 125
Val Gly Ala Leu Glu Lys Arg Leu Glu Ala Phe Gly Asp Gly Pro Trp
130 135 140
Ala Val Gly Gly Asn Met Thr Ile Ala Asp Leu His Ile Cys His Leu
145 150 155 160
Val Thr Asn Ile Arg Cys Gly Met Leu Asp Phe Val Asp Lys Asp Leu
165 170 175
Leu Glu Gly Tyr Val Arg Ile Val Lys Ser Tyr Ser Ala Val Met Glu
180 185 190
His Pro Lys Val Thr Glu Trp Tyr Glu Lys Lys Pro Val Lys Met Phe
195 200 205
Ser
<210> 27
<211> 396
<212> PRT
<213> Escherichia coli
<400> 27
Met Lys Ile Lys Thr Gly Ala Arg Ile Leu Ala Leu Ser Ala Leu Thr
1 5 10 15
Thr Met Met Phe Ser Ala Ser Ala Leu Ala Lys Ile Glu Glu Gly Lys
20 25 30
Leu Val Ile Trp Ile Asn Gly Asp Lys Gly Tyr Asn Gly Leu Ala Glu
35 40 45
Val Gly Lys Lys Phe Glu Lys Asp Thr Gly Ile Lys Val Thr Val Glu
50 55 60
His Pro Asp Lys Leu Glu Glu Lys Phe Pro Gln Val Ala Ala Thr Gly
65 70 75 80
Asp Gly Pro Asp Ile Ile Phe Trp Ala His Asp Arg Phe Gly Gly Tyr
85 90 95
Ala Gln Ser Gly Leu Leu Ala Glu Ile Thr Pro Asp Lys Ala Phe Gln
100 105 110
Asp Lys Leu Tyr Pro Phe Thr Trp Asp Ala Val Arg Tyr Asn Gly Lys
115 120 125
Leu Ile Ala Tyr Pro Ile Ala Val Glu Ala Leu Ser Leu Ile Tyr Asn
130 135 140
Lys Asp Leu Leu Pro Asn Pro Pro Lys Thr Trp Glu Glu Ile Pro Ala
145 150 155 160
Leu Asp Lys Glu Leu Lys Ala Lys Gly Lys Ser Ala Leu Met Phe Asn
165 170 175
Leu Gln Glu Pro Tyr Phe Thr Trp Pro Leu Ile Ala Ala Asp Gly Gly
180 185 190
Tyr Ala Phe Lys Tyr Glu Asn Gly Lys Tyr Asp Ile Lys Asp Val Gly
195 200 205
Val Asp Asn Ala Gly Ala Lys Ala Gly Leu Thr Phe Leu Val Asp Leu
210 215 220
Ile Lys Asn Lys His Met Asn Ala Asp Thr Asp Tyr Ser Ile Ala Glu
225 230 235 240
Ala Ala Phe Asn Lys Gly Glu Thr Ala Met Thr Ile Asn Gly Pro Trp
245 250 255
Ala Trp Ser Asn Ile Asp Thr Ser Lys Val Asn Tyr Gly Val Thr Val
260 265 270
Leu Pro Thr Phe Lys Gly Gln Pro Ser Lys Pro Phe Val Gly Val Leu
275 280 285
Ser Ala Gly Ile Asn Ala Ala Ser Pro Asn Lys Glu Leu Ala Lys Glu
290 295 300
Phe Leu Glu Asn Tyr Leu Leu Thr Asp Glu Gly Leu Glu Ala Val Asn
305 310 315 320
Lys Asp Lys Pro Leu Gly Ala Val Ala Leu Lys Ser Tyr Glu Glu Glu
325 330 335
Leu Ala Lys Asp Pro Arg Ile Ala Ala Thr Met Glu Asn Ala Gln Lys
340 345 350
Gly Glu Ile Met Pro Asn Ile Pro Gln Met Ser Ala Phe Trp Tyr Ala
355 360 365
Val Arg Thr Ala Val Ile Asn Ala Ala Ser Gly Arg Gln Thr Val Asp
370 375 380
Glu Ala Leu Lys Asp Ala Gln Thr Arg Ile Thr Lys
385 390 395
<210> 28
<211> 5
<212> PRT
<213> Artificial Sequence
<220>
<223> protease cleavage site
<400> 28
Pro Ala Pro Ser Pro
1 5
<210> 29
<211> 4
<212> PRT
<213> Artificial Sequence
<220>
<223> protease cleavage site
<400> 29
Pro Pro Ser Pro
1
<210> 30
<211> 4
<212> PRT
<213> Artificial Sequence
<220>
<223> protease cleavage site
<400> 30
Pro Pro Ala Pro
1
<210> 31
<211> 4
<212> PRT
<213> Artificial Sequence
<220>
<223> protease cleavage site
<400> 31
Pro Pro Thr Pro
1
<210> 32
<211> 4
<212> PRT
<213> Artificial Sequence
<220>
<223> protease cleavage site
<400> 32
Pro Pro Gly Pro
1
<210> 33
<211> 6
<212> PRT
<213> Artificial Sequence
<220>
<223> enzymatic cleavage site
<400> 33
Pro Arg Pro Pro Thr Pro
1 5
<210> 34
<211> 7
<212> PRT
<213> Artificial Sequence
<220>
<223> enzymatic cleavage site
<400> 34
Val Val Ala Pro Pro Ala Pro
1 5
<210> 35
<211> 7
<212> PRT
<213> Artificial Sequence
<220>
<223> enzymatic cleavage site
<400> 35
Val Val Ala Pro Pro Ser Pro
1 5
<210> 36
<211> 7
<212> PRT
<213> Artificial Sequence
<220>
<223> enzymatic cleavage site
<400> 36
Val Val Ala Pro Pro Thr Pro
1 5
<210> 37
<211> 7
<212> PRT
<213> Artificial Sequence
<220>
<223> enzymatic cleavage site
<400> 37
Val Val Ala Pro Pro Gly Pro
1 5
<210> 38
<211> 6
<212> PRT
<213> Artificial Sequence
<220>
<223> enzymatic cleavage site
<400> 38
Pro Arg Pro Pro Thr Pro
1 5
<210> 39
<211> 6
<212> PRT
<213> Artificial Sequence
<220>
<223> enzymatic cleavage site
<400> 39
Ala Pro Pro Ala Ala Pro
1 5
<210> 40
<211> 6
<212> PRT
<213> Artificial Sequence
<220>
<223> enzymatic cleavage site
<400> 40
Pro Arg Pro Pro Ala Pro
1 5
<210> 41
<211> 6
<212> PRT
<213> Artificial Sequence
<220>
<223> enzymatic cleavage site
<400> 41
Pro Arg Pro Pro Ser Pro
1 5
<210> 42
<211> 6
<212> PRT
<213> Artificial Sequence
<220>
<223> enzymatic cleavage site
<400> 42
Pro Arg Pro Pro Gly Pro
1 5
<210> 43
<211> 285
<212> PRT
<213> Artificial Sequence
<220>
<223> Tetranectin-apolipoprotein A-I (1)
<400> 43
Ala Pro Ile Val Asn Ala Lys Lys Asp Val Val Asn Thr Lys Met Phe
1 5 10 15
Glu Glu Leu Lys Ser Arg Leu Asp Thr Leu Ala Gln Glu Val Ala Leu
20 25 30
Leu Lys Glu Gln Gln Ala Leu Gln Thr Val Asp Glu Pro Pro Gln Ser
35 40 45
Pro Trp Asp Arg Val Lys Asp Leu Ala Thr Val Tyr Val Asp Val Leu
50 55 60
Lys Asp Ser Gly Arg Asp Tyr Val Ser Gln Phe Glu Gly Ser Ala Leu
65 70 75 80
Gly Lys Gln Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser Val Thr
85 90 95
Ser Thr Phe Ser Lys Leu Arg Glu Gln Leu Gly Pro Val Thr Gln Glu
100 105 110
Phe Trp Asp Asn Leu Glu Lys Glu Thr Glu Gly Leu Arg Gln Glu Met
115 120 125
Ser Lys Asp Leu Glu Glu Val Lys Ala Lys Val Gln Pro Tyr Leu Asp
130 135 140
Asp Phe Gln Lys Lys Trp Gln Glu Glu Met Glu Leu Tyr Arg Gln Lys
145 150 155 160
Val Glu Pro Leu Arg Ala Glu Leu Gln Glu Gly Ala Arg Gln Lys Leu
165 170 175
His Glu Leu Gln Glu Lys Leu Ser Pro Leu Gly Glu Glu Met Arg Asp
180 185 190
Arg Ala Arg Ala His Val Asp Ala Leu Arg Thr His Leu Ala Pro Tyr
195 200 205
Ser Asp Glu Leu Arg Gln Arg Leu Ala Ala Arg Leu Glu Ala Leu Lys
210 215 220
Glu Asn Gly Gly Ala Arg Leu Ala Glu Tyr His Ala Lys Ala Thr Glu
225 230 235 240
His Leu Ser Thr Leu Ser Glu Lys Ala Lys Pro Ala Leu Glu Asp Leu
245 250 255
Arg Gln Gly Leu Leu Pro Val Leu Glu Ser Phe Lys Val Ser Phe Leu
260 265 270
Ser Ala Leu Glu Glu Tyr Thr Lys Lys Leu Asn Thr Gln
275 280 285
<210> 44
<211> 283
<212> PRT
<213> Artificial Sequence
<220>
<223> Tetranectin-apolipoprotein A-I (2)
<400> 44
Ile Val Asn Ala Lys Lys Asp Val Val Asn Thr Lys Met Phe Glu Glu
1 5 10 15
Leu Lys Ser Arg Leu Asp Thr Leu Ala Gln Glu Val Ala Leu Leu Lys
20 25 30
Glu Gln Gln Ala Leu Gln Thr Val Asp Glu Pro Pro Gln Ser Pro Trp
35 40 45
Asp Arg Val Lys Asp Leu Ala Thr Val Tyr Val Asp Val Leu Lys Asp
50 55 60
Ser Gly Arg Asp Tyr Val Ser Gln Phe Glu Gly Ser Ala Leu Gly Lys
65 70 75 80
Gln Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser Val Thr Ser Thr
85 90 95
Phe Ser Lys Leu Arg Glu Gln Leu Gly Pro Val Thr Gln Glu Phe Trp
100 105 110
Asp Asn Leu Glu Lys Glu Thr Glu Gly Leu Arg Gln Glu Met Ser Lys
115 120 125
Asp Leu Glu Glu Val Lys Ala Lys Val Gln Pro Tyr Leu Asp Asp Phe
130 135 140
Gln Lys Lys Trp Gln Glu Glu Met Glu Leu Tyr Arg Gln Lys Val Glu
145 150 155 160
Pro Leu Arg Ala Glu Leu Gln Glu Gly Ala Arg Gln Lys Leu His Glu
165 170 175
Leu Gln Glu Lys Leu Ser Pro Leu Gly Glu Glu Met Arg Asp Arg Ala
180 185 190
Arg Ala His Val Asp Ala Leu Arg Thr His Leu Ala Pro Tyr Ser Asp
195 200 205
Glu Leu Arg Gln Arg Leu Ala Ala Arg Leu Glu Ala Leu Lys Glu Asn
210 215 220
Gly Gly Ala Arg Leu Ala Glu Tyr His Ala Lys Ala Thr Glu His Leu
225 230 235 240
Ser Thr Leu Ser Glu Lys Ala Lys Pro Ala Leu Glu Asp Leu Arg Gln
245 250 255
Gly Leu Leu Pro Val Leu Glu Ser Phe Lys Val Ser Phe Leu Ser Ala
260 265 270
Leu Glu Glu Tyr Thr Lys Lys Leu Asn Thr Gln
275 280
<210> 45
<211> 285
<212> PRT
<213> Artificial Sequence
<220>
<223> Tetranectin-apolipoprotein A-I
<220>
<221> MISC_FEATURE
<223> X = A or G or S or T
<220>
<221> misc_feature
<222> (1)..(1)
<223> Xaa can be any naturally occurring amino acid
<400> 45
Xaa Pro Ile Val Asn Ala Lys Lys Asp Val Val Asn Thr Lys Met Phe
1 5 10 15
Glu Glu Leu Lys Ser Arg Leu Asp Thr Leu Ala Gln Glu Val Ala Leu
20 25 30
Leu Lys Glu Gln Gln Ala Leu Gln Thr Val Asp Glu Pro Pro Gln Ser
35 40 45
Pro Trp Asp Arg Val Lys Asp Leu Ala Thr Val Tyr Val Asp Val Leu
50 55 60
Lys Asp Ser Gly Arg Asp Tyr Val Ser Gln Phe Glu Gly Ser Ala Leu
65 70 75 80
Gly Lys Gln Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser Val Thr
85 90 95
Ser Thr Phe Ser Lys Leu Arg Glu Gln Leu Gly Pro Val Thr Gln Glu
100 105 110
Phe Trp Asp Asn Leu Glu Lys Glu Thr Glu Gly Leu Arg Gln Glu Met
115 120 125
Ser Lys Asp Leu Glu Glu Val Lys Ala Lys Val Gln Pro Tyr Leu Asp
130 135 140
Asp Phe Gln Lys Lys Trp Gln Glu Glu Met Glu Leu Tyr Arg Gln Lys
145 150 155 160
Val Glu Pro Leu Arg Ala Glu Leu Gln Glu Gly Ala Arg Gln Lys Leu
165 170 175
His Glu Leu Gln Glu Lys Leu Ser Pro Leu Gly Glu Glu Met Arg Asp
180 185 190
Arg Ala Arg Ala His Val Asp Ala Leu Arg Thr His Leu Ala Pro Tyr
195 200 205
Ser Asp Glu Leu Arg Gln Arg Leu Ala Ala Arg Leu Glu Ala Leu Lys
210 215 220
Glu Asn Gly Gly Ala Arg Leu Ala Glu Tyr His Ala Lys Ala Thr Glu
225 230 235 240
His Leu Ser Thr Leu Ser Glu Lys Ala Lys Pro Ala Leu Glu Asp Leu
245 250 255
Arg Gln Gly Leu Leu Pro Val Leu Glu Ser Phe Lys Val Ser Phe Leu
260 265 270
Ser Ala Leu Glu Glu Tyr Thr Lys Lys Leu Asn Thr Gln
275 280 285
<210> 46
<211> 22
<212> PRT
<213> Artificial Sequence
<220>
<223> Apolipoprotein A-I mimetic (1)
<400> 46
Pro Val Leu Asp Glu Phe Arg Glu Lys Leu Asn Glu Glu Leu Glu Ala
1 5 10 15
Leu Lys Gln Lys Leu Lys
20
<210> 47
<211> 22
<212> PRT
<213> Artificial Sequence
<220>
<223> Apolipoprotein A-I mimetic (2)
<400> 47
Pro Val Leu Asp Leu Phe Arg Glu Leu Leu Asn Glu Leu Leu Glu Ala
1 5 10 15
Leu Lys Gln Lys Leu Lys
20
<210> 48
<211> 267
<212> PRT
<213> Homo sapiens
<400> 48
Met Lys Ala Ala Val Leu Thr Leu Ala Val Leu Phe Leu Thr Gly Ser
1 5 10 15
Gln Ala Arg His Phe Trp Gln Gln Asp Glu Pro Pro Gln Ser Pro Trp
20 25 30
Asp Arg Val Lys Asp Leu Ala Thr Val Tyr Val Asp Val Leu Lys Asp
35 40 45
Ser Gly Arg Asp Tyr Val Ser Gln Phe Glu Gly Ser Ala Leu Gly Lys
50 55 60
Gln Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser Val Thr Ser Thr
65 70 75 80
Phe Ser Lys Leu Arg Glu Gln Leu Gly Pro Val Thr Gln Glu Phe Trp
85 90 95
Asp Asn Leu Glu Lys Glu Thr Glu Gly Leu Arg Gln Glu Met Ser Lys
100 105 110
Asp Leu Glu Glu Val Lys Ala Lys Val Gln Pro Tyr Leu Asp Asp Phe
115 120 125
Gln Lys Lys Trp Gln Glu Glu Met Glu Leu Tyr Arg Gln Lys Val Glu
130 135 140
Pro Leu Arg Ala Glu Leu Gln Glu Gly Ala Arg Gln Lys Leu His Glu
145 150 155 160
Leu Gln Glu Lys Leu Ser Pro Leu Gly Glu Glu Met Arg Asp Arg Ala
165 170 175
Arg Ala His Val Asp Ala Leu Arg Thr His Leu Ala Pro Tyr Ser Asp
180 185 190
Glu Leu Arg Gln Arg Leu Ala Ala Arg Leu Glu Ala Leu Lys Glu Asn
195 200 205
Gly Gly Ala Arg Leu Ala Glu Tyr His Ala Lys Ala Thr Glu His Leu
210 215 220
Ser Thr Leu Ser Glu Lys Ala Lys Pro Ala Leu Glu Asp Leu Arg Gln
225 230 235 240
Gly Leu Leu Pro Val Leu Glu Ser Phe Lys Val Ser Phe Leu Ser Ala
245 250 255
Leu Glu Glu Tyr Thr Lys Lys Leu Asn Thr Gln
260 265
<210> 49
<211> 100
<212> PRT
<213> Homo sapiens
<400> 49
Met Lys Leu Leu Ala Ala Thr Val Leu Leu Leu Thr Ile Cys Ser Leu
1 5 10 15
Glu Gly Ala Leu Val Arg Arg Gln Ala Lys Glu Pro Cys Val Glu Ser
20 25 30
Leu Val Ser Gln Tyr Phe Gln Thr Val Thr Asp Tyr Gly Lys Asp Leu
35 40 45
Met Glu Lys Val Lys Ser Pro Glu Leu Gln Ala Glu Ala Lys Ser Tyr
50 55 60
Phe Glu Lys Ser Lys Glu Gln Leu Thr Pro Leu Ile Lys Lys Ala Gly
65 70 75 80
Thr Glu Leu Val Asn Phe Leu Ser Tyr Phe Val Glu Leu Gly Thr Gln
85 90 95
Pro Ala Thr Gln
100
<210> 50
<211> 396
<212> PRT
<213> Homo sapiens
<400> 50
Met Phe Leu Lys Ala Val Val Leu Thr Leu Ala Leu Val Ala Val Ala
1 5 10 15
Gly Ala Arg Ala Glu Val Ser Ala Asp Gln Val Ala Thr Val Met Trp
20 25 30
Asp Tyr Phe Ser Gln Leu Ser Asn Asn Ala Lys Glu Ala Val Glu His
35 40 45
Leu Gln Lys Ser Glu Leu Thr Gln Gln Leu Asn Ala Leu Phe Gln Asp
50 55 60
Lys Leu Gly Glu Val Asn Thr Tyr Ala Gly Asp Leu Gln Lys Lys Leu
65 70 75 80
Val Pro Phe Ala Thr Glu Leu His Glu Arg Leu Ala Lys Asp Ser Glu
85 90 95
Lys Leu Lys Glu Glu Ile Gly Lys Glu Leu Glu Glu Leu Arg Ala Arg
100 105 110
Leu Leu Pro His Ala Asn Glu Val Ser Gln Lys Ile Gly Asp Asn Leu
115 120 125
Arg Glu Leu Gln Gln Arg Leu Glu Pro Tyr Ala Asp Gln Leu Arg Thr
130 135 140
Gln Val Asn Thr Gln Ala Glu Gln Leu Arg Arg Gln Leu Thr Pro Tyr
145 150 155 160
Ala Gln Arg Met Glu Arg Val Leu Arg Glu Asn Ala Asp Ser Leu Gln
165 170 175
Ala Ser Leu Arg Pro His Ala Asp Glu Leu Lys Ala Lys Ile Asp Gln
180 185 190
Asn Val Glu Glu Leu Lys Gly Arg Leu Thr Pro Tyr Ala Asp Glu Phe
195 200 205
Lys Val Lys Ile Asp Gln Thr Val Glu Glu Leu Arg Arg Ser Leu Ala
210 215 220
Pro Tyr Ala Gln Asp Thr Gln Glu Lys Leu Asn His Gln Leu Glu Gly
225 230 235 240
Leu Thr Phe Gln Met Lys Lys Asn Ala Glu Glu Leu Lys Ala Arg Ile
245 250 255
Ser Ala Ser Ala Glu Glu Leu Arg Gln Arg Leu Ala Pro Leu Ala Glu
260 265 270
Asp Val Arg Gly Asn Leu Arg Gly Asn Thr Glu Gly Leu Gln Lys Ser
275 280 285
Leu Ala Glu Leu Gly Gly His Leu Asp Gln Gln Val Glu Glu Phe Arg
290 295 300
Arg Arg Val Glu Pro Tyr Gly Glu Asn Phe Asn Lys Ala Leu Val Gln
305 310 315 320
Gln Met Glu Gln Leu Arg Gln Lys Leu Gly Pro His Ala Gly Asp Val
325 330 335
Glu Gly His Leu Ser Phe Leu Glu Lys Asp Leu Arg Asp Lys Val Asn
340 345 350
Ser Phe Phe Ser Thr Phe Lys Glu Lys Glu Ser Gln Asp Lys Thr Leu
355 360 365
Ser Leu Pro Glu Leu Glu Gln Gln Gln Glu Gln Gln Gln Glu Gln Gln
370 375 380
Gln Glu Gln Val Gln Met Leu Ala Pro Leu Glu Ser
385 390 395
<210> 51
<211> 366
<212> PRT
<213> Homo sapiens
<400> 51
Met Ala Ser Met Ala Ala Val Leu Thr Trp Ala Leu Ala Leu Leu Ser
1 5 10 15
Ala Phe Ser Ala Thr Gln Ala Arg Lys Gly Phe Trp Asp Tyr Phe Ser
20 25 30
Gln Thr Ser Gly Asp Lys Gly Arg Val Glu Gln Ile His Gln Gln Lys
35 40 45
Met Ala Arg Glu Pro Ala Thr Leu Lys Asp Ser Leu Glu Gln Asp Leu
50 55 60
Asn Asn Met Asn Lys Phe Leu Glu Lys Leu Arg Pro Leu Ser Gly Ser
65 70 75 80
Glu Ala Pro Arg Leu Pro Gln Asp Pro Val Gly Met Arg Arg Gln Leu
85 90 95
Gln Glu Glu Leu Glu Glu Val Lys Ala Arg Leu Gln Pro Tyr Met Ala
100 105 110
Glu Ala His Glu Leu Val Gly Trp Asn Leu Glu Gly Leu Arg Gln Gln
115 120 125
Leu Lys Pro Tyr Thr Met Asp Leu Met Glu Gln Val Ala Leu Arg Val
130 135 140
Gln Glu Leu Gln Glu Gln Leu Arg Val Val Gly Glu Asp Thr Lys Ala
145 150 155 160
Gln Leu Leu Gly Gly Val Asp Glu Ala Trp Ala Leu Leu Gln Gly Leu
165 170 175
Gln Ser Arg Val Val His His Thr Gly Arg Phe Lys Glu Leu Phe His
180 185 190
Pro Tyr Ala Glu Ser Leu Val Ser Gly Ile Gly Arg His Val Gln Glu
195 200 205
Leu His Arg Ser Val Ala Pro His Ala Pro Ala Ser Pro Ala Arg Leu
210 215 220
Ser Arg Cys Val Gln Val Leu Ser Arg Lys Leu Thr Leu Lys Ala Lys
225 230 235 240
Ala Leu His Ala Arg Ile Gln Gln Asn Leu Asp Gln Leu Arg Glu Glu
245 250 255
Leu Ser Arg Ala Phe Ala Gly Thr Gly Thr Glu Glu Gly Ala Gly Pro
260 265 270
Asp Pro Gln Met Leu Ser Glu Glu Val Arg Gln Arg Leu Gln Ala Phe
275 280 285
Arg Gln Asp Thr Tyr Leu Gln Ile Ala Ala Phe Thr Arg Ala Ile Asp
290 295 300
Gln Glu Thr Glu Glu Val Gln Gln Gln Leu Ala Pro Pro Pro Pro Gly
305 310 315 320
His Ser Ala Phe Ala Pro Glu Phe Gln Gln Thr Asp Ser Gly Lys Val
325 330 335
Leu Ser Lys Leu Gln Ala Arg Leu Asp Asp Leu Trp Glu Asp Ile Thr
340 345 350
His Ser Leu His Asp Gln Gly His Ser His Leu Gly Asp Pro
355 360 365
<210> 52
<211> 267
<212> PRT
<213> Homo sapiens
<400> 52
Met Lys Ala Ala Val Leu Thr Leu Ala Val Leu Phe Leu Thr Gly Ser
1 5 10 15
Gln Ala Arg His Phe Trp Gln Gln Asp Glu Pro Pro Gln Ser Pro Trp
20 25 30
Asp Arg Val Lys Asp Leu Ala Thr Val Tyr Val Asp Val Leu Lys Asp
35 40 45
Ser Gly Arg Asp Tyr Val Ser Gln Phe Glu Gly Ser Ala Leu Gly Lys
50 55 60
Gln Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser Val Thr Ser Thr
65 70 75 80
Phe Ser Lys Leu Arg Glu Gln Leu Gly Pro Val Thr Gln Glu Phe Trp
85 90 95
Asp Asn Leu Glu Lys Glu Thr Glu Gly Leu Arg Gln Glu Met Ser Lys
100 105 110
Asp Leu Glu Glu Val Lys Ala Lys Val Gln Pro Tyr Leu Asp Asp Phe
115 120 125
Gln Lys Lys Trp Gln Glu Glu Met Glu Leu Tyr Arg Gln Lys Val Glu
130 135 140
Pro Leu Arg Ala Glu Leu Gln Glu Gly Ala Arg Gln Lys Leu His Glu
145 150 155 160
Leu Gln Glu Lys Leu Ser Pro Leu Gly Glu Glu Met Arg Asp Arg Ala
165 170 175
Arg Ala His Val Asp Ala Leu Arg Thr His Leu Ala Pro Tyr Ser Asp
180 185 190
Glu Leu Arg Gln Arg Leu Ala Ala Arg Leu Glu Ala Leu Lys Glu Asn
195 200 205
Gly Gly Ala Arg Leu Ala Glu Tyr His Ala Lys Ala Thr Glu His Leu
210 215 220
Ser Thr Leu Ser Glu Lys Ala Lys Pro Ala Leu Glu Asp Leu Arg Gln
225 230 235 240
Gly Leu Leu Pro Val Leu Glu Ser Phe Lys Val Ser Phe Leu Ser Ala
245 250 255
Leu Glu Glu Tyr Thr Lys Lys Leu Asn Thr Gln
260 265
<210> 53
<211> 267
<212> PRT
<213> Homo sapiens
<400> 53
Met Lys Ala Ala Val Leu Thr Leu Ala Val Leu Phe Leu Thr Gly Ser
1 5 10 15
Gln Ala Arg His Phe Trp Gln Gln Asp Glu Pro Pro Gln Ser Pro Trp
20 25 30
Asp Arg Val Lys Asp Leu Ala Thr Val Tyr Val Asp Val Leu Lys Asp
35 40 45
Ser Gly Arg Asp Tyr Val Ser Gln Phe Glu Gly Ser Ala Leu Gly Lys
50 55 60
Gln Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser Val Thr Ser Thr
65 70 75 80
Phe Ser Lys Leu Arg Glu Gln Leu Gly Pro Val Thr Gln Glu Phe Trp
85 90 95
Asp Asn Leu Glu Lys Glu Thr Glu Gly Leu Arg Gln Glu Met Ser Lys
100 105 110
Asp Leu Glu Glu Val Lys Ala Lys Val Gln Pro Tyr Leu Asp Asp Phe
115 120 125
Gln Lys Lys Trp Gln Glu Glu Met Glu Leu Tyr Arg Gln Lys Val Glu
130 135 140
Pro Leu Arg Ala Glu Leu Gln Glu Gly Ala Arg Gln Lys Leu His Glu
145 150 155 160
Leu Gln Glu Lys Leu Ser Pro Leu Gly Glu Glu Met Arg Asp Arg Ala
165 170 175
Arg Ala His Val Asp Ala Leu Arg Thr His Leu Ala Pro Tyr Ser Asp
180 185 190
Glu Leu Arg Gln Arg Leu Ala Ala Arg Leu Glu Ala Leu Lys Glu Asn
195 200 205
Gly Gly Ala Arg Leu Ala Glu Tyr His Ala Lys Ala Thr Glu His Leu
210 215 220
Ser Thr Leu Ser Glu Lys Ala Lys Pro Ala Leu Glu Asp Leu Arg Gln
225 230 235 240
Gly Leu Leu Pro Val Leu Glu Ser Phe Lys Val Ser Phe Leu Ser Ala
245 250 255
Leu Glu Glu Tyr Thr Lys Lys Leu Asn Thr Gln
260 265
<210> 54
<211> 267
<212> PRT
<213> Homo sapiens
<400> 54
Met Lys Ala Thr Val Leu Thr Leu Ala Val Leu Phe Leu Thr Gly Ser
1 5 10 15
Gln Ala Arg His Phe Trp Gln Gln Asp Glu Pro Pro Gln Thr Pro Trp
20 25 30
Asp Arg Val Lys Asp Leu Val Thr Val Tyr Val Glu Ala Leu Lys Asp
35 40 45
Ser Gly Lys Asp Tyr Val Ser Gln Phe Glu Gly Ser Ala Leu Gly Lys
50 55 60
Gln Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser Val Thr Ser Thr
65 70 75 80
Val Ser Lys Leu Arg Glu Gln Leu Gly Pro Val Thr Gln Glu Phe Trp
85 90 95
Asp Asn Leu Glu Lys Glu Thr Glu Gly Leu Arg Gln Glu Met Ser Lys
100 105 110
Asp Leu Glu Glu Val Lys Ala Lys Val Gln Pro Tyr Leu Asp Asp Phe
115 120 125
Gln Lys Lys Trp Gln Glu Glu Met Glu Leu Tyr Arg Gln Lys Val Glu
130 135 140
Pro Leu Arg Ala Glu Leu His Glu Gly Thr Arg Gln Lys Leu His Glu
145 150 155 160
Leu His Glu Lys Leu Ser Pro Leu Gly Glu Glu Val Arg Asp Arg Ala
165 170 175
Arg Ala His Val Asp Ala Leu Arg Thr His Leu Ala Pro Tyr Ser Asp
180 185 190
Glu Leu Arg Gln Arg Leu Ala Ala Arg Leu Glu Ala Leu Lys Glu Asn
195 200 205
Gly Gly Ala Arg Leu Ala Glu Tyr His Ala Lys Ala Ser Glu His Leu
210 215 220
Ser Thr Leu Ser Glu Lys Ala Lys Pro Ala Leu Glu Asp Leu Arg Gln
225 230 235 240
Gly Leu Leu Pro Val Leu Glu Ser Phe Lys Val Ser Phe Leu Ser Ala
245 250 255
Leu Glu Glu Tyr Thr Lys Lys Leu Ser Thr Gln
260 265
<210> 55
<211> 265
<212> PRT
<213> Homo sapiens
<400> 55
Met Lys Ala Val Val Leu Thr Leu Ala Val Leu Phe Leu Thr Gly Ser
1 5 10 15
Gln Ala Arg His Phe Trp Gln Gln Asp Asp Pro Gln Ser Ser Trp Asp
20 25 30
Arg Val Lys Asp Phe Ala Thr Val Tyr Val Glu Ala Ile Lys Asp Ser
35 40 45
Gly Arg Asp Tyr Val Ala Gln Phe Glu Ala Ser Ala Leu Gly Lys Gln
50 55 60
Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp Thr Leu Ala Ser Thr Leu
65 70 75 80
Ser Lys Val Arg Glu Gln Leu Gly Pro Val Thr Gln Glu Phe Trp Asp
85 90 95
Asn Leu Glu Lys Glu Thr Ala Ser Leu Arg Gln Glu Met His Lys Asp
100 105 110
Leu Glu Glu Val Lys Gln Lys Val Gln Pro Tyr Leu Asp Glu Phe Gln
115 120 125
Lys Lys Trp His Glu Glu Val Glu Ile Tyr Arg Gln Lys Val Ala Pro
130 135 140
Leu Gly Glu Glu Phe Arg Glu Gly Ala Arg Gln Lys Val Gln Glu Leu
145 150 155 160
Gln Asp Lys Leu Ser Pro Leu Ala Gln Glu Leu Arg Asp Arg Ala Arg
165 170 175
Ala His Val Glu Thr Leu Arg Gln Gln Leu Ala Pro Tyr Ser Asp Asp
180 185 190
Leu Arg Gln Arg Leu Thr Ala Arg Leu Glu Ala Leu Lys Glu Gly Gly
195 200 205
Gly Ser Leu Ala Glu Tyr His Ala Lys Ala Ser Glu Gln Leu Lys Ala
210 215 220
Leu Gly Glu Lys Ala Lys Pro Val Leu Glu Asp Leu Arg Gln Gly Leu
225 230 235 240
Leu Pro Val Leu Glu Ser Leu Lys Val Ser Ile Leu Ala Ala Ile Asp
245 250 255
Glu Ala Ser Lys Lys Leu Asn Ala Gln
260 265
<210> 56
<211> 264
<212> PRT
<213> Homo sapiens
<400> 56
Met Lys Ala Trp Leu Thr Leu Ala Val Leu Phe Leu Thr Gly Ser Gln
1 5 10 15
Ala Arg His Phe Trp Gln Gln Asp Asp Pro Gln Ser Pro Trp Asp Arg
20 25 30
Val Lys Asp Phe Ala Thr Val Tyr Val Asp Ala Ile Lys Asp Ser Gly
35 40 45
Arg Asp Tyr Val Ala Gln Phe Glu Ala Ser Ala Leu Gly Lys His Leu
50 55 60
Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser Leu Gly Ser Thr Phe Thr
65 70 75 80
Lys Val Arg Glu Gln Leu Gly Pro Val Thr Gln Glu Phe Trp Asp Asn
85 90 95
Leu Glu Lys Glu Thr Glu Ala Leu Arg Gln Glu Met Ser Lys Asp Leu
100 105 110
Glu Glu Val Lys Lys Lys Val Gln Pro Tyr Leu Asp Asp Phe Gln Asn
115 120 125
Lys Trp Gln Glu Glu Met Glu Thr Tyr Arg Gln Lys Met Ala Pro Leu
130 135 140
Gly Ala Glu Phe Arg Glu Gly Ala Arg Gln Lys Val Gln Glu Leu Gln
145 150 155 160
Glu Lys Leu Ser Pro Leu Ala Glu Glu Leu Arg Asp Arg Leu Arg Ala
165 170 175
His Val Glu Ala Leu Arg Gln His Val Ala Pro Tyr Ser Asp Asp Leu
180 185 190
Arg Gln Arg Met Ala Ala Arg Phe Glu Ala Leu Lys Glu Gly Gly Gly
195 200 205
Ser Leu Ala Glu Tyr Gln Ala Lys Ala Gln Glu Gln Leu Lys Ala Leu
210 215 220
Gly Glu Lys Ala Lys Pro Ala Leu Glu Asp Leu Arg Gln Gly Leu Leu
225 230 235 240
Pro Val Leu Glu Asn Leu Lys Val Ser Ile Leu Ala Ala Ile Asp Glu
245 250 255
Ala Ser Lys Lys Leu Asn Ala Gln
260
<210> 57
<211> 266
<212> PRT
<213> Homo sapiens
<400> 57
Met Lys Ala Ala Leu Leu Thr Leu Ala Val Leu Phe Leu Thr Gly Ser
1 5 10 15
Gln Ala Arg His Phe Trp Gln Gln Asp Glu Pro Gln Ser Pro Trp Asp
20 25 30
Arg Val Lys Asp Leu Ala Thr Val Tyr Val Asp Ala Val Lys Asp Ser
35 40 45
Gly Arg Asp Tyr Val Ala Gln Phe Glu Ala Ser Ala Leu Gly Lys Gln
50 55 60
Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser Leu Ser Ser Thr Val
65 70 75 80
Thr Lys Leu Arg Glu Gln Ile Gly Pro Val Thr Gln Glu Phe Trp Asp
85 90 95
Asn Leu Glu Lys Glu Thr Glu Val Leu Arg Gln Glu Met Ser Lys Asp
100 105 110
Leu Glu Glu Val Lys Gln Lys Val Gln Pro Tyr Leu Asp Asp Phe Gln
115 120 125
Lys Lys Trp Gln Glu Glu Val Glu Leu Tyr Arg Gln Lys Val Ala Pro
130 135 140
Leu Gly Ser Glu Leu Arg Glu Gly Ala Arg Gln Lys Leu Gln Glu Leu
145 150 155 160
Gln Glu Lys Leu Ser Pro Leu Ala Glu Glu Leu Arg Asp Arg Ala Arg
165 170 175
Thr His Val Asp Ala Leu Arg Ala Gln Leu Ala Pro Tyr Ser Asp Asp
180 185 190
Leu Arg Glu Arg Leu Ala Ala Arg Leu Glu Ala Leu Lys Glu Gly Gly
195 200 205
Gly Ala Ser Leu Ala Glu Tyr His Ala Arg Ala Ser Glu Gln Leu Ser
210 215 220
Ala Leu Gly Glu Lys Ala Arg Pro Ala Leu Glu Asp Leu Arg Gln Gly
225 230 235 240
Leu Leu Pro Val Leu Glu Ser Phe Lys Val Ser Leu Leu Ala Ala Ile
245 250 255
Asp Glu Ala Thr Lys Lys Leu Asn Ala Gln
260 265
<210> 58
<211> 206
<212> PRT
<213> Homo sapiens
<400> 58
Met Lys Ala Val Val Leu Thr Leu Ala Val Leu Phe Leu Thr Gly Ser
1 5 10 15
Gln Ala Arg His Phe Trp Gln Arg Asp Glu Pro Arg Ser Ser Trp Asp
20 25 30
Lys Ile Lys Asp Phe Ala Thr Val Tyr Val Asp Thr Val Lys Asp Ser
35 40 45
Gly Arg Glu Tyr Val Ala Gln Phe Glu Ala Ser Ala Phe Gly Lys Gln
50 55 60
Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser Leu Ser Ser Thr Val
65 70 75 80
Ser Lys Leu Gln Glu Gln Leu Gly Pro Val Thr Gln Glu Phe Trp Asp
85 90 95
Asn Leu Glu Lys Glu Thr Glu Gly Leu Arg Glu Glu Met Asn Lys Asp
100 105 110
Leu Gln Glu Val Arg Gln Lys Val Gln Pro Tyr Leu Asp Glu Phe Gln
115 120 125
Lys Lys Trp Gln Glu Glu Val Glu Arg Tyr Arg Gln Lys Val Glu Pro
130 135 140
Leu Gly Ala Glu Leu Arg Glu Ser Ala Arg Gln Lys Leu Thr Glu Leu
145 150 155 160
Gln Glu Lys Leu Ser Pro Leu Ala Glu Glu Leu Arg Asp Ser Ala Arg
165 170 175
Thr His Val Gly Leu Leu Pro Val Leu Glu Ser Phe Lys Ala Ser Val
180 185 190
Gln Asn Val Leu Asp Glu Ala Thr Lys Lys Leu Asn Thr Gln
195 200 205
<210> 59
<211> 265
<212> PRT
<213> Homo sapiens
<400> 59
Met Lys Ala Val Val Leu Thr Leu Ala Val Leu Phe Leu Thr Gly Ser
1 5 10 15
Gln Ala Arg His Phe Trp Gln Gln Asp Glu Pro Gln Ser Ser Trp Asp
20 25 30
Arg Val Arg Asp Leu Ala Asn Val Tyr Val Asp Ala Val Lys Glu Ser
35 40 45
Gly Arg Glu Tyr Val Ser Gln Leu Glu Ala Ser Ala Leu Gly Lys Gln
50 55 60
Leu Asn Leu Lys Leu Val Asp Asn Trp Asp Thr Leu Gly Ser Thr Phe
65 70 75 80
Gln Lys Val His Glu His Leu Gly Pro Val Ala Gln Glu Phe Trp Glu
85 90 95
Lys Leu Glu Lys Glu Thr Glu Glu Leu Arg Arg Glu Ile Asn Lys Asp
100 105 110
Leu Glu Asp Val Arg Gln Lys Thr Gln Pro Phe Leu Asp Glu Ile Gln
115 120 125
Lys Lys Trp Gln Glu Asp Leu Glu Arg Tyr Arg Gln Lys Val Glu Pro
130 135 140
Leu Ser Ala Gln Leu Arg Glu Gly Ala Arg Gln Lys Leu Met Glu Leu
145 150 155 160
Gln Glu Gln Val Thr Pro Leu Gly Glu Asp Leu Arg Asp Ser Val Arg
165 170 175
Ala Tyr Ala Asp Thr Leu Arg Thr Gln Leu Ala Pro Tyr Ser Glu Gln
180 185 190
Met Arg Lys Thr Leu Gly Ala Arg Leu Glu Ala Ile Lys Glu Gly Gly
195 200 205
Ser Ala Ser Leu Ala Glu Tyr His Ala Lys Ala Ser Glu Gln Leu Ser
210 215 220
Ala Leu Gly Glu Lys Ala Lys Pro Val Leu Glu Asp Ile His Gln Gly
225 230 235 240
Leu Met Pro Met Trp Glu Ser Phe Lys Thr Gly Val Leu Asn Val Ile
245 250 255
Asp Glu Ala Ala Lys Lys Leu Thr Ala
260 265
<210> 60
<211> 264
<212> PRT
<213> Homo sapiens
<400> 60
Met Lys Ala Val Val Leu Ala Val Ala Leu Val Phe Leu Thr Gly Ser
1 5 10 15
Gln Ala Trp His Val Trp Gln Gln Asp Glu Pro Gln Ser Gln Trp Asp
20 25 30
Lys Val Lys Asp Phe Ala Asn Val Tyr Val Asp Ala Val Lys Asp Ser
35 40 45
Gly Arg Asp Tyr Val Ser Gln Phe Glu Ser Ser Ser Leu Gly Gln Gln
50 55 60
Leu Asn Leu Asn Leu Leu Glu Asn Trp Asp Thr Leu Gly Ser Thr Val
65 70 75 80
Ser Gln Leu Gln Glu Arg Leu Gly Pro Leu Thr Arg Asp Phe Trp Asp
85 90 95
Asn Leu Glu Lys Glu Thr Asp Trp Val Arg Gln Glu Met Asn Lys Asp
100 105 110
Leu Glu Glu Val Lys Gln Lys Val Gln Pro Tyr Leu Asp Glu Phe Gln
115 120 125
Lys Lys Trp Lys Glu Asp Val Glu Leu Tyr Arg Gln Lys Val Ala Pro
130 135 140
Leu Gly Ala Glu Leu Gln Glu Ser Ala Arg Gln Lys Leu Gln Glu Leu
145 150 155 160
Gln Gly Arg Leu Ser Pro Val Ala Glu Glu Phe Arg Asp Arg Met Arg
165 170 175
Thr His Val Asp Ser Leu Arg Thr Gln Leu Ala Pro His Ser Glu Gln
180 185 190
Met Arg Glu Ser Leu Ala Gln Arg Leu Ala Glu Leu Lys Ser Asn Pro
195 200 205
Thr Leu Asn Glu Tyr His Thr Arg Ala Lys Thr His Leu Lys Thr Leu
210 215 220
Gly Glu Lys Ala Arg Pro Ala Leu Glu Asp Leu Arg His Ser Leu Met
225 230 235 240
Pro Met Leu Glu Thr Leu Lys Thr Lys Ala Gln Ser Val Ile Asp Lys
245 250 255
Ala Ser Glu Thr Leu Thr Ala Gln
260
<210> 61
<211> 259
<212> PRT
<213> Homo sapiens
<400> 61
Met Lys Ala Ala Val Leu Ala Val Ala Leu Val Phe Leu Thr Gly Cys
1 5 10 15
Gln Ala Trp Glu Phe Trp Gln Gln Asp Glu Pro Gln Ser Gln Trp Asp
20 25 30
Arg Val Lys Asp Phe Ala Thr Val Tyr Val Asp Ala Val Lys Asp Ser
35 40 45
Gly Arg Asp Tyr Val Ser Gln Phe Glu Ser Ser Thr Leu Gly Lys Gln
50 55 60
Leu Asn Leu Asn Leu Leu Asp Asn Trp Asp Thr Leu Gly Ser Thr Val
65 70 75 80
Gly Arg Leu Gln Glu Gln Leu Gly Pro Val Thr Gln Glu Phe Trp Ala
85 90 95
Asn Leu Glu Lys Glu Thr Asp Trp Leu Arg Asn Glu Met Asn Lys Asp
100 105 110
Leu Glu Asn Val Lys Gln Lys Met Gln Pro His Leu Asp Glu Phe Gln
115 120 125
Glu Lys Trp Asn Glu Glu Val Glu Ala Tyr Arg Gln Lys Leu Glu Pro
130 135 140
Leu Gly Thr Glu Leu His Lys Asn Ala Lys Glu Met Gln Arg His Leu
145 150 155 160
Lys Val Val Ala Glu Glu Phe Arg Asp Arg Met Arg Val Asn Ala Asp
165 170 175
Ala Leu Arg Ala Lys Phe Gly Leu Tyr Ser Asp Gln Met Arg Glu Asn
180 185 190
Leu Ala Gln Arg Leu Thr Glu Ile Arg Asn His Pro Thr Leu Ile Glu
195 200 205
Tyr His Thr Lys Ala Gly Asp His Leu Arg Thr Leu Gly Glu Lys Ala
210 215 220
Lys Pro Ala Leu Asp Asp Leu Gly Gln Gly Leu Met Pro Val Leu Glu
225 230 235 240
Ala Trp Lys Ala Lys Ile Met Ser Met Ile Asp Glu Ala Lys Lys Lys
245 250 255
Leu Asn Ala
<210> 62
<211> 241
<212> PRT
<213> Homo sapiens
<400> 62
Asp Glu Ala Lys Ser Tyr Trp Asp Gln Ile Lys Asp Met Leu Thr Val
1 5 10 15
Tyr Val Asp Thr Ala Lys Asp Ser Gly Lys Asp Tyr Leu Thr Ser Leu
20 25 30
Asp Thr Ser Ala Leu Gly Gln Gln Leu Asn Lys Lys Leu Ala Asp Asn
35 40 45
Trp Asp Thr Val Ser Ser Ala Leu Leu Lys Ala Arg Glu Gln Met Lys
50 55 60
Pro Ile Ala Met Glu Phe Trp Gly Asn Leu Glu Lys Asp Thr Glu Gly
65 70 75 80
Leu Arg Gln Thr Val Ser Lys Asp Leu Glu Leu Val Lys Glu Lys Val
85 90 95
Gln Pro Tyr Leu Asp Ser Phe Gln Lys Lys Val Glu Glu Glu Leu Glu
100 105 110
Leu Tyr Arg Gln Lys Val Ala Pro Leu Ser Ala Glu Trp Arg Glu Gln
115 120 125
Ala Arg Gln Lys Ala Gln Glu Leu Gln Gln Lys Ala Gly Glu Leu Gly
130 135 140
Gln Gln His Arg Asp Arg Val Arg Thr His Val Asp Ala Leu Arg Thr
145 150 155 160
Asp Leu Ala Pro Tyr Gly Glu Glu Ala Arg Lys Leu Leu Leu Gln Arg
165 170 175
Leu Gln Asp Ile Lys Ala Lys Ser Gly Asp Leu Ala Glu Tyr Gln Thr
180 185 190
Lys Leu Ser Glu His Leu Lys Ser Phe Gly Glu Lys Ala Gln Pro Thr
195 200 205
Leu Gln Asp Leu Arg His Gly Leu Glu Pro Leu Trp Glu Gly Ile Lys
210 215 220
Ala Gly Ala Met Ser Met Leu Glu Glu Leu Gly Lys Lys Leu Asn Ser
225 230 235 240
Gln
<210> 63
<211> 264
<212> PRT
<213> Homo sapiens
<400> 63
Met Arg Gly Val Leu Val Thr Leu Ala Val Leu Phe Leu Thr Gly Thr
1 5 10 15
Gln Ala Arg Ser Phe Trp Gln His Asp Glu Pro Gln Thr Pro Leu Asp
20 25 30
Arg Ile Arg Asp Met Val Asp Val Tyr Leu Glu Thr Val Lys Ala Ser
35 40 45
Gly Lys Asp Ala Ile Ala Gln Phe Glu Ser Ser Ala Val Gly Lys Gln
50 55 60
Leu Asp Leu Lys Leu Ala Asp Asn Leu Asp Thr Leu Ser Ala Ala Ala
65 70 75 80
Ala Lys Leu Arg Glu Asp Met Ala Pro Tyr Tyr Lys Glu Val Arg Glu
85 90 95
Met Trp Leu Lys Asp Thr Glu Ala Leu Arg Ala Glu Leu Thr Lys Asp
100 105 110
Leu Glu Glu Val Lys Glu Lys Ile Arg Pro Phe Leu Asp Gln Phe Ser
115 120 125
Ala Lys Trp Thr Glu Glu Leu Glu Gln Tyr Arg Gln Arg Leu Thr Pro
130 135 140
Val Ala Gln Glu Leu Lys Glu Leu Thr Lys Gln Lys Val Glu Leu Met
145 150 155 160
Gln Ala Lys Leu Thr Pro Val Ala Glu Glu Ala Arg Asp Arg Leu Arg
165 170 175
Gly His Val Glu Glu Leu Arg Lys Asn Leu Ala Pro Tyr Ser Asp Glu
180 185 190
Leu Arg Gln Lys Leu Ser Gln Lys Leu Glu Glu Ile Arg Glu Lys Gly
195 200 205
Ile Pro Gln Ala Ser Glu Tyr Gln Ala Lys Val Met Glu Gln Leu Ser
210 215 220
Asn Leu Arg Glu Lys Met Thr Pro Leu Val Gln Glu Phe Arg Glu Arg
225 230 235 240
Leu Thr Pro Tyr Ala Glu Asn Leu Lys Asn Arg Leu Ile Ser Phe Leu
245 250 255
Asp Glu Leu Gln Lys Ser Val Ala
260
<210> 64
<211> 264
<212> PRT
<213> Homo sapiens
<400> 64
Met Arg Gly Val Leu Val Thr Leu Ala Val Leu Phe Leu Thr Gly Thr
1 5 10 15
Gln Ala Arg Ser Phe Trp Gln His Asp Asp Pro Gln Thr Pro Leu Asp
20 25 30
Arg Ile Arg Asp Met Leu Asp Val Tyr Leu Glu Thr Val Lys Ala Ser
35 40 45
Gly Lys Asp Ala Ile Ser Gln Phe Glu Ser Ser Ala Val Gly Lys Gln
50 55 60
Leu Asp Leu Lys Leu Ala Asp Asn Leu Asp Thr Leu Ser Ala Ala Ala
65 70 75 80
Ala Lys Leu Arg Glu Asp Met Thr Pro Tyr Tyr Arg Glu Val Arg Glu
85 90 95
Met Trp Leu Lys Asp Thr Glu Ala Leu Arg Ala Glu Leu Thr Lys Asp
100 105 110
Leu Glu Glu Val Lys Glu Lys Ile Arg Pro Phe Leu Asp Gln Phe Ser
115 120 125
Ala Lys Trp Thr Glu Glu Val Glu Gln Tyr Arg Gln Arg Leu Ala Pro
130 135 140
Val Ala Gln Glu Leu Lys Asp Leu Thr Lys Gln Lys Val Glu Leu Met
145 150 155 160
Gln Ala Lys Leu Thr Pro Val Ala Glu Glu Val Arg Asp Arg Leu Arg
165 170 175
Glu Gln Val Glu Glu Leu Arg Lys Asn Leu Ala Pro Tyr Ser Ser Glu
180 185 190
Leu Arg Gln Lys Leu Ser Gln Lys Leu Glu Glu Ile Arg Glu Arg Gly
195 200 205
Ile Pro Gln Ala Ser Glu Tyr Gln Ala Lys Val Val Glu Gln Leu Ser
210 215 220
Asn Leu Arg Glu Lys Met Thr Pro Leu Val Gln Glu Phe Lys Glu Arg
225 230 235 240
Leu Thr Pro Tyr Ala Glu Asn Leu Lys Asn Arg Leu Ile Asp Leu Leu
245 250 255
Asp Glu Val Gln Lys Thr Met Ala
260
<210> 65
<211> 264
<212> PRT
<213> Homo sapiens
<400> 65
Met Arg Val Val Val Val Thr Leu Ala Leu Leu Phe Leu Thr Gly Thr
1 5 10 15
Gln Ala Arg Tyr Phe Trp Gln His Asp Glu Pro Gln Ala Pro Leu Asp
20 25 30
Arg Leu Arg Asp Leu Val Asp Val Tyr Leu Glu Thr Val Lys Ala Ser
35 40 45
Gly Lys Asp Ala Ile Ala Gln Phe Glu Ala Ser Ala Val Gly Lys Gln
50 55 60
Leu Asp Leu Lys Leu Ala Asp Asn Leu Asp Thr Leu Gly Ala Ala Ala
65 70 75 80
Ala Lys Leu Arg Glu Asp Met Ala Pro Tyr Tyr Lys Glu Val Arg Glu
85 90 95
Met Trp Leu Lys Asp Thr Glu Ser Leu Arg Ala Glu Leu Thr Lys Asp
100 105 110
Leu Glu Glu Val Lys Glu Lys Ile Arg Pro Phe Leu Asp Gln Phe Ser
115 120 125
Ala Lys Trp Thr Glu Glu Leu Glu Gln Tyr Arg Gln Arg Leu Ala Pro
130 135 140
Val Ala Glu Glu Leu Lys Glu Leu Thr Lys Gln Lys Val Glu Leu Met
145 150 155 160
Gln Gln Lys Leu Thr Pro Val Ala Glu Glu Ala Arg Asp Arg Leu Arg
165 170 175
Gly His Val Glu Glu Leu Arg Lys Asn Leu Ala Pro Tyr Ser Asp Glu
180 185 190
Leu Arg Gln Lys Leu Ser Gln Lys Leu Glu Glu Ile Arg Glu Lys Gly
195 200 205
Ile Pro Gln Ala Ala Glu Tyr Gln Ala Lys Val Val Glu Gln Leu Ser
210 215 220
Asn Leu Arg Glu Lys Met Thr Pro Leu Val Gln Asp Phe Lys Glu Arg
225 230 235 240
Leu Thr Pro Tyr Ala Glu Asn Leu Lys Thr Arg Phe Ile Ser Leu Leu
245 250 255
Asp Glu Leu Gln Lys Thr Val Ala
260
<210> 66
<211> 262
<212> PRT
<213> Homo sapiens
<400> 66
Met Lys Phe Leu Ala Leu Ala Leu Thr Ile Leu Leu Ala Ala Gly Thr
1 5 10 15
Gln Ala Phe Pro Met Gln Ala Asp Ala Pro Ser Gln Leu Glu His Val
20 25 30
Lys Ala Ala Leu Ser Met Tyr Ile Ala Gln Val Lys Leu Thr Ala Gln
35 40 45
Arg Ser Ile Asp Leu Leu Asp Asp Thr Glu Tyr Lys Glu Tyr Lys Met
50 55 60
Gln Leu Thr Gln Ser Leu Asp Asn Leu Gln Gln Tyr Ala Asp Ala Thr
65 70 75 80
Ser Gln Ser Leu Ala Pro Tyr Ser Glu Ala Phe Gly Thr Gln Leu Thr
85 90 95
Asp Ala Thr Ala Ala Val Arg Ala Glu Val Met Lys Asp Val Glu Glu
100 105 110
Leu Arg Ser Gln Leu Glu Pro Lys Arg Ala Glu Leu Lys Glu Val Leu
115 120 125
Asp Lys His Ile Asp Glu Tyr Arg Lys Lys Leu Glu Pro Leu Ile Lys
130 135 140
Glu His Ile Glu Leu Arg Arg Thr Glu Met Glu Ala Phe Arg Ala Lys
145 150 155 160
Met Glu Pro Ile Val Glu Glu Leu Arg Ala Lys Val Ala Ile Asn Val
165 170 175
Glu Glu Thr Lys Thr Lys Leu Met Pro Ile Val Glu Ile Val Arg Ala
180 185 190
Lys Leu Thr Glu Arg Leu Glu Glu Leu Arg Thr Leu Ala Ala Pro Tyr
195 200 205
Ala Glu Glu Tyr Lys Glu Gln Met Ile Lys Ala Val Gly Glu Val Arg
210 215 220
Glu Lys Val Ser Pro Leu Ser Glu Asp Phe Lys Gly Gln Val Gly Pro
225 230 235 240
Ala Ala Glu Gln Ala Lys Gln Lys Leu Leu Ala Phe Tyr Glu Thr Ile
245 250 255
Ser Gln Ala Met Lys Ala
260
<210> 67
<211> 262
<212> PRT
<213> Homo sapiens
<400> 67
Met Lys Phe Leu Ala Leu Ala Leu Thr Ile Leu Leu Ala Ala Ala Thr
1 5 10 15
Gln Ala Val Pro Met Gln Ala Asp Ala Pro Ser Gln Leu Glu His Val
20 25 30
Lys Val Ala Met Met Glu Tyr Met Ala Gln Val Lys Glu Thr Gly Gln
35 40 45
Arg Ser Ile Asp Leu Leu Asp Asp Thr Glu Phe Lys Glu Tyr Lys Val
50 55 60
Gln Leu Ser Gln Ser Leu Asp Asn Leu Gln Gln Tyr Ala Gln Thr Thr
65 70 75 80
Ser Gln Ser Leu Ala Pro Tyr Ser Glu Ala Phe Gly Ala Gln Leu Thr
85 90 95
Asp Ala Ala Ala Ala Val Arg Ala Glu Val Met Lys Asp Val Glu Asp
100 105 110
Val Arg Thr Gln Leu Glu Pro Lys Arg Ala Glu Leu Lys Glu Val Leu
115 120 125
Asp Lys His Ile Asp Glu Tyr Arg Lys Lys Leu Glu Pro Leu Ile Lys
130 135 140
Glu Ile Val Glu Gln Arg Arg Thr Glu Leu Glu Ala Phe Arg Val Lys
145 150 155 160
Met Glu Pro Val Val Glu Glu Met Arg Ala Lys Val Ser Thr Asn Val
165 170 175
Glu Glu Thr Lys Ala Lys Leu Met Pro Ile Val Glu Thr Val Arg Ala
180 185 190
Lys Leu Thr Glu Arg Leu Glu Glu Leu Arg Thr Leu Ala Ala Pro Tyr
195 200 205
Ala Glu Glu Tyr Lys Glu Gln Met Phe Lys Ala Val Gly Glu Val Arg
210 215 220
Glu Lys Val Gly Pro Leu Thr Asn Asp Phe Lys Gly Gln Val Gly Pro
225 230 235 240
Ala Ala Glu Gln Ala Lys Glu Lys Leu Met Asp Phe Tyr Glu Thr Ile
245 250 255
Ser Gln Ala Met Lys Ala
260
<210> 68
<211> 258
<212> PRT
<213> Homo sapiens
<400> 68
Met Lys Phe Leu Val Leu Ala Leu Thr Ile Leu Leu Ala Ala Gly Thr
1 5 10 15
Gln Ala Phe Pro Met Gln Ala Asp Ala Pro Ser Gln Leu Glu His Val
20 25 30
Lys Ala Ala Leu Asn Met Tyr Ile Ala Gln Val Lys Leu Thr Ala Gln
35 40 45
Arg Ser Ile Asp Leu Leu Asp Asp Thr Glu Tyr Lys Glu Tyr Lys Met
50 55 60
Gln Leu Ser Gln Ser Leu Asp Asn Leu Gln Gln Phe Ala Asp Ser Thr
65 70 75 80
Ser Lys Ser Trp Pro Pro Thr Pro Arg Ser Ser Ala Pro Ser Cys Asp
85 90 95
Ala Thr Ala Thr Val Arg Ala Glu Val Met Lys Asp Val Glu Asp Val
100 105 110
Arg Thr Gln Leu Glu Pro Lys Arg Ala Glu Leu Thr Glu Val Leu Asn
115 120 125
Lys His Ile Asp Glu Tyr Arg Lys Lys Leu Glu Pro Leu Ile Lys Gln
130 135 140
His Ile Glu Leu Arg Arg Thr Glu Met Asp Ala Phe Arg Ala Lys Ile
145 150 155 160
Asp Pro Val Val Glu Glu Met Arg Ala Lys Val Ala Val Asn Val Glu
165 170 175
Glu Thr Lys Thr Lys Leu Met Pro Ile Val Glu Ile Val Arg Ala Lys
180 185 190
Leu Thr Glu Arg Leu Glu Glu Leu Arg Thr Leu Ala Ala Pro Tyr Ala
195 200 205
Glu Glu Tyr Lys Glu Gln Met Phe Lys Ala Val Gly Glu Val Arg Glu
210 215 220
Lys Val Ala Pro Leu Ser Glu Asp Phe Lys Ala Arg Trp Ala Pro Pro
225 230 235 240
Pro Arg Arg Pro Ser Lys Ser Ser Trp Leu Ser Thr Arg Pro Ser Ala
245 250 255
Arg Pro
<210> 69
<211> 262
<212> PRT
<213> Homo sapiens
<400> 69
Met Lys Phe Val Ala Leu Ala Leu Thr Leu Leu Leu Ala Leu Gly Ser
1 5 10 15
Gln Ala Asn Leu Phe Gln Ala Asp Ala Pro Thr Gln Leu Glu His Tyr
20 25 30
Lys Ala Ala Ala Leu Val Tyr Leu Asn Gln Val Lys Asp Gln Ala Glu
35 40 45
Lys Ala Leu Asp Asn Leu Asp Gly Thr Asp Tyr Glu Gln Tyr Lys Leu
50 55 60
Gln Leu Ser Glu Ser Leu Thr Lys Leu Gln Glu Tyr Ala Gln Thr Thr
65 70 75 80
Ser Gln Ala Leu Thr Pro Tyr Ala Glu Thr Ile Ser Thr Gln Leu Met
85 90 95
Glu Asn Thr Lys Gln Leu Arg Glu Arg Val Met Thr Asp Val Glu Asp
100 105 110
Leu Arg Ser Lys Leu Glu Pro His Arg Ala Glu Leu Tyr Thr Ala Leu
115 120 125
Gln Lys His Ile Asp Glu Tyr Arg Glu Lys Leu Glu Pro Val Phe Gln
130 135 140
Glu Tyr Ser Ala Leu Asn Arg Gln Asn Ala Glu Gln Leu Arg Ala Lys
145 150 155 160
Leu Glu Pro Leu Met Asp Asp Ile Arg Lys Ala Phe Glu Ser Asn Ile
165 170 175
Glu Glu Thr Lys Ser Lys Val Val Pro Met Val Glu Ala Val Arg Thr
180 185 190
Lys Leu Thr Glu Arg Leu Glu Asp Leu Arg Thr Met Ala Ala Pro Tyr
195 200 205
Ala Glu Glu Tyr Lys Glu Gln Leu Val Lys Ala Val Glu Glu Ala Arg
210 215 220
Glu Lys Ile Ala Pro His Thr Gln Asp Leu Gln Thr Arg Met Glu Pro
225 230 235 240
Tyr Met Glu Asn Val Arg Thr Thr Phe Ala Gln Met Tyr Glu Thr Ile
245 250 255
Ala Lys Ala Ile Gln Ala
260
<210> 70
<211> 260
<212> PRT
<213> Homo sapiens
<400> 70
Met Lys Phe Ala Ala Leu Ala Leu Ala Leu Leu Leu Ala Val Gly Ser
1 5 10 15
His Ala Ala Ser Met Gln Ala Asp Ala Pro Ser Gln Leu Asp His Ala
20 25 30
Arg Ala Val Leu Asp Val Tyr Leu Thr Gln Val Lys Asp Met Ser Leu
35 40 45
Arg Ala Val Asn Gln Leu Asp Asp Pro Gln Tyr Ala Glu Phe Lys Thr
50 55 60
Asn Leu Ala Gln Arg Ile Glu Glu Met Tyr Thr Gln Ile Lys Thr Leu
65 70 75 80
Gln Gly Ser Val Ser Pro Met Thr Asp Ser Phe Tyr Asn Thr Val Met
85 90 95
Glu Val Thr Lys Asp Thr Arg Glu Ser Leu Asn Val Asp Leu Glu Ala
100 105 110
Leu Lys Ser Ser Leu Ala Pro Gln Asn Glu Gln Leu Lys Gln Val Ile
115 120 125
Glu Lys His Leu Asn Asp Tyr Arg Thr Leu Leu Thr Pro Ile Tyr Asn
130 135 140
Asp Tyr Lys Thr Lys His Asp Glu Glu Met Ala Ala Leu Lys Thr Arg
145 150 155 160
Leu Glu Pro Val Met Glu Glu Leu Arg Thr Lys Ile Gln Ala Asn Val
165 170 175
Glu Glu Thr Lys Ala Val Leu Met Pro Met Val Glu Thr Val Arg Thr
180 185 190
Lys Val Thr Glu Arg Leu Glu Ser Leu Arg Glu Val Val Gln Pro Tyr
195 200 205
Val Gln Glu Tyr Lys Glu Gln Met Lys Gln Met Tyr Asp Gln Ala Gln
210 215 220
Thr Val Asp Thr Asp Ala Leu Arg Thr Lys Ile Thr Pro Leu Val Glu
225 230 235 240
Glu Ile Lys Val Lys Met Asn Ala Ile Phe Glu Ile Ile Ala Ala Ser
245 250 255
Val Thr Lys Ser
260
<210> 71
<211> 396
<212> PRT
<213> Homo sapiens
<400> 71
Met Phe Leu Lys Ala Val Val Leu Thr Leu Ala Leu Val Ala Val Ala
1 5 10 15
Gly Ala Arg Ala Glu Val Ser Ala Asp Gln Val Ala Thr Val Met Trp
20 25 30
Asp Tyr Phe Ser Gln Leu Ser Asn Asn Ala Lys Glu Ala Val Glu His
35 40 45
Leu Gln Lys Ser Glu Leu Thr Gln Gln Leu Asn Ala Leu Phe Gln Asp
50 55 60
Lys Leu Gly Glu Val Asn Thr Tyr Ala Gly Asp Leu Gln Lys Lys Leu
65 70 75 80
Val Pro Phe Ala Thr Glu Leu His Glu Arg Leu Ala Lys Asp Ser Glu
85 90 95
Lys Leu Lys Glu Glu Ile Gly Lys Glu Leu Glu Glu Leu Arg Ala Arg
100 105 110
Leu Leu Pro His Ala Asn Glu Val Ser Gln Lys Ile Gly Asp Asn Leu
115 120 125
Arg Glu Leu Gln Gln Arg Leu Glu Pro Tyr Ala Asp Gln Leu Arg Thr
130 135 140
Gln Val Asn Thr Gln Ala Glu Gln Leu Arg Arg Gln Leu Thr Pro Tyr
145 150 155 160
Ala Gln Arg Met Glu Arg Val Leu Arg Glu Asn Ala Asp Ser Leu Gln
165 170 175
Ala Ser Leu Arg Pro His Ala Asp Glu Leu Lys Ala Lys Ile Asp Gln
180 185 190
Asn Val Glu Glu Leu Lys Gly Arg Leu Thr Pro Tyr Ala Asp Glu Phe
195 200 205
Lys Val Lys Ile Asp Gln Thr Val Glu Glu Leu Arg Arg Ser Leu Ala
210 215 220
Pro Tyr Ala Gln Asp Thr Gln Glu Lys Leu Asn His Gln Leu Glu Gly
225 230 235 240
Leu Thr Phe Gln Met Lys Lys Asn Ala Glu Glu Leu Lys Ala Arg Ile
245 250 255
Ser Ala Ser Ala Glu Glu Leu Arg Gln Arg Leu Ala Pro Leu Ala Glu
260 265 270
Asp Val Arg Gly Asn Leu Lys Gly Asn Thr Glu Gly Leu Gln Lys Ser
275 280 285
Leu Ala Glu Leu Gly Gly His Leu Asp Gln Gln Val Glu Glu Phe Arg
290 295 300
Arg Arg Val Glu Pro Tyr Gly Glu Asn Phe Asn Lys Ala Leu Val Gln
305 310 315 320
Gln Met Glu Gln Leu Arg Gln Lys Leu Gly Pro His Ala Gly Asp Val
325 330 335
Glu Gly His Leu Ser Phe Leu Glu Lys Asp Leu Arg Asp Lys Val Asn
340 345 350
Ser Phe Phe Ser Thr Phe Lys Glu Lys Glu Ser Gln Asp Lys Thr Leu
355 360 365
Ser Leu Pro Glu Leu Glu Gln Gln Gln Glu Gln Gln Gln Glu Gln Gln
370 375 380
Gln Glu Gln Val Gln Met Leu Ala Pro Leu Glu Ser
385 390 395
<210> 72
<211> 429
<212> PRT
<213> Homo sapiens
<400> 72
Met Phe Leu Lys Ala Val Val Leu Thr Leu Ala Leu Val Ala Val Thr
1 5 10 15
Gly Ala Arg Ala Glu Val Ser Ala Asp Gln Val Ala Thr Val Met Trp
20 25 30
Asp Tyr Phe Ser Gln Leu Ser Ser Asn Ala Lys Glu Ala Val Glu His
35 40 45
Leu Gln Lys Ser Glu Leu Thr Gln Gln Leu Asn Ala Leu Phe Gln Asp
50 55 60
Lys Leu Gly Glu Val Asn Thr Tyr Ala Gly Asp Leu Gln Lys Lys Leu
65 70 75 80
Val Pro Phe Ala Thr Glu Leu His Glu Arg Leu Ala Lys Asp Ser Glu
85 90 95
Lys Leu Lys Glu Glu Ile Arg Lys Glu Leu Glu Glu Val Arg Ala Arg
100 105 110
Leu Leu Pro His Ala Asn Glu Val Ser Gln Lys Ile Gly Glu Asn Val
115 120 125
Arg Glu Leu Gln Gln Arg Leu Glu Pro Tyr Thr Asp Gln Leu Arg Thr
130 135 140
Gln Val Asn Thr Gln Thr Glu Gln Leu Arg Arg Gln Leu Thr Pro Tyr
145 150 155 160
Ala Gln Arg Met Glu Arg Val Leu Arg Glu Asn Ala Asp Ser Leu Gln
165 170 175
Thr Ser Leu Arg Pro His Ala Asp Gln Leu Lys Ala Lys Ile Asp Gln
180 185 190
Asn Val Glu Glu Leu Lys Glu Arg Leu Thr Pro Tyr Ala Asp Glu Phe
195 200 205
Lys Val Lys Ile Asp Gln Thr Val Glu Glu Leu Arg Arg Ser Leu Ala
210 215 220
Pro Tyr Ala Gln Asp Ala Gln Glu Lys Leu Asn His Gln Leu Glu Gly
225 230 235 240
Leu Ala Phe Gln Met Lys Lys Asn Ala Glu Glu Leu Lys Ala Arg Ile
245 250 255
Ser Ala Ser Ala Glu Glu Leu Arg Gln Arg Leu Ala Pro Leu Ala Glu
260 265 270
Asp Met Arg Gly Asn Leu Arg Gly Asn Thr Glu Gly Leu Gln Lys Ser
275 280 285
Leu Ala Glu Leu Gly Gly His Leu Asp Arg His Val Glu Glu Phe Arg
290 295 300
Leu Arg Val Glu Pro Tyr Gly Glu Asn Phe Asn Lys Ala Leu Val Gln
305 310 315 320
Gln Met Glu Gln Leu Arg Gln Lys Leu Gly Pro His Ala Gly Asp Val
325 330 335
Glu Gly His Leu Ser Phe Leu Glu Lys Asp Leu Arg Asp Lys Val Asn
340 345 350
Ser Phe Phe Ser Thr Phe Lys Glu Lys Glu Ser Gln Asp Asn Thr Leu
355 360 365
Ser Leu Pro Glu Pro Glu Gln Gln Arg Glu Gln Gln Gln Glu Gln Gln
370 375 380
Gln Glu Gln Glu Gln Glu Gln Gln Gln Gln Gln Glu Gln Gln Gln Gln
385 390 395 400
Gln Glu Gln Gln Arg Glu Gln Gln Gln Gln Glu Gln Gln Gln Glu Gln
405 410 415
Gln Gln Glu Gln Val Gln Met Leu Ala Pro Leu Glu Ser
420 425
<210> 73
<211> 395
<212> PRT
<213> Homo sapiens
<400> 73
Met Phe Leu Lys Ala Ala Val Leu Thr Leu Ala Leu Val Ala Ile Thr
1 5 10 15
Gly Thr Arg Ala Glu Val Thr Ser Asp Gln Val Ala Asn Val Val Trp
20 25 30
Asp Tyr Phe Thr Gln Leu Ser Asn Asn Ala Lys Glu Ala Val Glu Gln
35 40 45
Phe Gln Lys Thr Asp Val Thr Gln Gln Leu Ser Thr Leu Phe Gln Asp
50 55 60
Lys Leu Gly Asp Ala Ser Thr Tyr Ala Asp Gly Val His Asn Lys Leu
65 70 75 80
Val Pro Phe Val Val Gln Leu Ser Gly His Leu Ala Lys Glu Thr Glu
85 90 95
Arg Val Lys Glu Glu Ile Lys Lys Glu Leu Glu Asp Leu Arg Asp Arg
100 105 110
Met Met Pro His Ala Asn Lys Val Thr Gln Thr Phe Gly Glu Asn Met
115 120 125
Gln Lys Leu Gln Glu His Leu Lys Pro Tyr Ala Val Asp Leu Gln Asp
130 135 140
Gln Ile Asn Thr Gln Thr Gln Glu Met Lys Leu Gln Leu Thr Pro Tyr
145 150 155 160
Ile Gln Arg Met Gln Thr Thr Ile Lys Glu Asn Val Asp Asn Leu His
165 170 175
Thr Ser Met Met Pro Leu Ala Thr Asn Leu Lys Asp Lys Phe Asn Arg
180 185 190
Asn Met Glu Glu Leu Lys Gly His Leu Thr Pro Arg Ala Asn Glu Leu
195 200 205
Lys Ala Thr Ile Asp Gln Asn Leu Glu Asp Leu Arg Arg Ser Leu Ala
210 215 220
Pro Leu Thr Val Gly Val Gln Glu Lys Leu Asn His Gln Met Glu Gly
225 230 235 240
Leu Ala Phe Gln Met Lys Lys Asn Ala Glu Glu Leu Gln Thr Lys Val
245 250 255
Ser Ala Lys Ile Asp Gln Leu Gln Lys Asn Leu Ala Pro Leu Val Glu
260 265 270
Asp Val Gln Ser Lys Val Lys Gly Asn Thr Glu Gly Leu Gln Lys Ser
275 280 285
Leu Glu Asp Leu Asn Arg Gln Leu Glu Gln Gln Val Glu Glu Phe Arg
290 295 300
Arg Thr Val Glu Pro Met Gly Glu Met Phe Asn Lys Ala Leu Val Gln
305 310 315 320
Gln Leu Glu Gln Phe Arg Gln Gln Leu Gly Pro Asn Ser Gly Glu Val
325 330 335
Glu Ser His Leu Ser Phe Leu Glu Lys Ser Leu Arg Glu Lys Val Asn
340 345 350
Ser Phe Met Ser Thr Leu Glu Lys Lys Gly Ser Pro Asp Gln Pro Gln
355 360 365
Ala Leu Pro Leu Pro Glu Gln Ala Gln Glu Gln Ala Gln Glu Gln Ala
370 375 380
Gln Glu Gln Val Gln Pro Lys Pro Leu Glu Ser
385 390 395
<210> 74
<211> 401
<212> PRT
<213> Homo sapiens
<400> 74
Gly Ala Arg Ala Glu Val Ser Ala Asp Gln Val Ala Thr Val Met Trp
1 5 10 15
Asp Tyr Phe Ser Gln Leu Ser Ser Asn Ala Lys Glu Ala Val Glu His
20 25 30
Leu Gln Lys Ser Glu Leu Thr Gln Gln Leu Asn Ala Leu Phe Gln Asp
35 40 45
Lys Leu Gly Glu Val Asn Thr Tyr Ala Gly Asp Leu Gln Lys Lys Leu
50 55 60
Val Pro Phe Ala Thr Glu Leu His Glu Arg Leu Ala Lys Asp Ser Lys
65 70 75 80
Lys Leu Lys Glu Glu Ile Arg Lys Glu Leu Glu Glu Val Arg Ala Arg
85 90 95
Leu Leu Pro His Ala Asn Glu Val Ser Gln Lys Ile Gly Glu Asn Val
100 105 110
Arg Glu Leu Gln Gln Arg Leu Glu Pro Tyr Thr Asp Gln Leu Arg Thr
115 120 125
Gln Val Asn Thr Gln Thr Glu Gln Leu Arg Arg Gln Leu Thr Pro Tyr
130 135 140
Ala Gln Arg Met Glu Arg Val Leu Arg Glu Asn Ala Asp Ser Leu Gln
145 150 155 160
Thr Ser Leu Arg Pro His Ala Asp Gln Leu Lys Ala Lys Ile Asp Gln
165 170 175
Asn Val Glu Glu Leu Lys Gly Arg Leu Thr Pro Tyr Ala Asp Glu Phe
180 185 190
Lys Val Lys Ile Asp Gln Thr Val Glu Glu Leu Arg Arg Ser Leu Ala
195 200 205
Pro Tyr Ala Gln Asp Ala Gln Glu Lys Leu Asn His Gln Leu Glu Gly
210 215 220
Leu Ala Phe Gln Met Lys Lys Asn Ala Glu Glu Leu Lys Ala Arg Ile
225 230 235 240
Ser Ala Ser Ala Glu Glu Leu Arg Gln Arg Leu Ala Pro Leu Ala Glu
245 250 255
Asp Met Arg Gly Asn Leu Arg Gly Asn Thr Glu Gly Leu Gln Lys Ser
260 265 270
Leu Ala Glu Leu Gly Gly His Leu Asp Arg His Val Glu Glu Phe Arg
275 280 285
Leu Arg Val Glu Pro Tyr Gly Glu Asn Phe Asn Lys Ala Leu Val Gln
290 295 300
Gln Met Glu Gln Leu Arg Gln Lys Leu Gly Pro His Ala Gly Asp Val
305 310 315 320
Glu Gly His Leu Ser Phe Leu Glu Lys Asp Leu Arg Asp Lys Val Asn
325 330 335
Ser Phe Phe Ser Thr Phe Lys Glu Lys Glu Ser Gln Asp Asn Thr Leu
340 345 350
Ser Leu Pro Glu Pro Glu Gln Gln Gln Glu Gln Gln Gln Glu Gln Glu
355 360 365
Gln Gln Gln Glu Gln Gln Glu Glu Gln Gln Gln Gln Glu Gln Gln Gln
370 375 380
Glu Gln Glu Gln Gln Gln Glu Gln Val Gln Met Leu Ala Pro Leu Glu
385 390 395 400
Ser
<210> 75
<211> 382
<212> PRT
<213> Homo sapiens
<400> 75
Met Phe Leu Lys Ala Val Val Leu Ser Leu Ala Leu Val Ala Val Thr
1 5 10 15
Gly Ala Arg Ala Glu Val Asn Ala Asp Gln Val Ala Thr Val Met Trp
20 25 30
Asp Tyr Phe Ser Gln Leu Gly Ser Asn Ala Lys Lys Ala Val Glu His
35 40 45
Leu Gln Lys Ser Glu Leu Thr Gln Gln Leu Asn Thr Leu Phe Gln Asp
50 55 60
Lys Leu Gly Glu Val Asn Thr Tyr Thr Glu Asp Leu Gln Lys Lys Leu
65 70 75 80
Val Pro Phe Ala Thr Glu Leu His Glu Arg Leu Thr Lys Asp Ser Glu
85 90 95
Lys Leu Lys Glu Glu Ile Arg Arg Glu Leu Glu Glu Leu Arg Ala Arg
100 105 110
Leu Leu Pro His Ala Thr Glu Val Ser Gln Lys Ile Gly Asp Asn Val
115 120 125
Arg Glu Leu Gln Gln Arg Leu Gly Pro Phe Thr Gly Gly Leu Arg Thr
130 135 140
Gln Val Asn Thr Gln Val Gln Gln Leu Gln Arg Gln Leu Lys Pro Tyr
145 150 155 160
Ala Glu Arg Met Glu Ser Val Leu Arg Gln Asn Ile Arg Asn Leu Glu
165 170 175
Ala Ser Val Ala Pro Tyr Ala Asp Glu Phe Lys Ala Lys Ile Asp Gln
180 185 190
Asn Val Glu Glu Leu Lys Gly Ser Leu Thr Pro Tyr Ala Glu Glu Leu
195 200 205
Lys Ala Lys Ile Asp Gln Asn Val Glu Glu Leu Arg Arg Ser Leu Ala
210 215 220
Pro Tyr Ala Gln Asp Val Gln Glu Lys Leu Asn His Gln Leu Glu Gly
225 230 235 240
Leu Ala Phe Gln Met Lys Lys Gln Ala Glu Glu Leu Lys Ala Lys Ile
245 250 255
Ser Ala Asn Ala Asp Glu Leu Arg Gln Lys Leu Val Pro Val Ala Glu
260 265 270
Asn Val His Gly His Leu Lys Gly Asn Thr Glu Gly Leu Gln Lys Ser
275 280 285
Leu Leu Glu Leu Arg Ser His Leu Asp Gln Gln Val Glu Glu Phe Arg
290 295 300
Leu Lys Val Glu Pro Tyr Gly Glu Thr Phe Asn Lys Ala Leu Val Gln
305 310 315 320
Gln Val Glu Asp Leu Arg Gln Lys Leu Gly Pro Leu Ala Gly Asp Val
325 330 335
Glu Gly His Leu Ser Phe Leu Glu Lys Asp Leu Arg Asp Lys Val Asn
340 345 350
Thr Phe Phe Ser Thr Leu Lys Glu Glu Ala Ser Gln Gly Gln Ser Gln
355 360 365
Ala Leu Pro Ala Gln Glu Lys Ala Gln Ala Pro Leu Glu Gly
370 375 380
<210> 76
<211> 391
<212> PRT
<213> Homo sapiens
<400> 76
Met Phe Leu Lys Ala Val Val Leu Thr Val Ala Leu Val Ala Ile Thr
1 5 10 15
Gly Thr Gln Ala Glu Val Thr Ser Asp Gln Val Ala Asn Val Met Trp
20 25 30
Asp Tyr Phe Thr Gln Leu Ser Asn Asn Ala Lys Glu Ala Val Glu Gln
35 40 45
Leu Gln Lys Thr Asp Val Thr Gln Gln Leu Asn Thr Leu Phe Gln Asp
50 55 60
Lys Leu Gly Asn Ile Asn Thr Tyr Ala Asp Asp Leu Gln Asn Lys Leu
65 70 75 80
Val Pro Phe Ala Val Gln Leu Ser Gly His Leu Thr Lys Glu Thr Glu
85 90 95
Arg Val Arg Glu Glu Ile Gln Lys Glu Leu Glu Asp Leu Arg Ala Asn
100 105 110
Met Met Pro His Ala Asn Lys Val Ser Gln Met Phe Gly Asp Asn Val
115 120 125
Gln Lys Leu Gln Glu His Leu Arg Pro Tyr Ala Thr Asp Leu Gln Ala
130 135 140
Gln Ile Asn Ala Gln Thr Gln Asp Met Lys Arg Gln Leu Thr Pro Tyr
145 150 155 160
Ile Gln Arg Met Gln Thr Thr Ile Gln Asp Asn Val Glu Asn Leu Gln
165 170 175
Ser Ser Met Val Pro Phe Ala Asn Glu Leu Lys Glu Lys Phe Asn Gln
180 185 190
Asn Met Glu Gly Leu Lys Gly Gln Leu Thr Pro Arg Ala Asn Glu Leu
195 200 205
Lys Ala Thr Ile Asp Gln Asn Leu Glu Asp Leu Arg Ser Arg Leu Ala
210 215 220
Pro Leu Ala Glu Gly Val Gln Glu Lys Leu Asn His Gln Met Glu Gly
225 230 235 240
Leu Ala Phe Gln Met Lys Lys Asn Ala Glu Glu Leu Gln Thr Lys Val
245 250 255
Ser Thr Asn Ile Asp Gln Leu Gln Lys Asn Leu Ala Pro Leu Val Glu
260 265 270
Asp Val Gln Ser Lys Leu Lys Gly Asn Thr Glu Gly Leu Gln Lys Ser
275 280 285
Leu Glu Asp Leu Asn Lys Gln Leu Asp Gln Gln Val Glu Val Phe Arg
290 295 300
Arg Ala Val Glu Pro Leu Gly Asp Lys Phe Asn Met Ala Leu Val Gln
305 310 315 320
Gln Met Glu Lys Phe Arg Gln Gln Leu Gly Ser Asp Ser Gly Asp Val
325 330 335
Glu Ser His Leu Ser Phe Leu Glu Lys Asn Leu Arg Glu Lys Val Ser
340 345 350
Ser Phe Met Ser Thr Leu Gln Lys Lys Gly Ser Pro Asp Gln Pro Leu
355 360 365
Ala Leu Pro Leu Pro Glu Gln Val Gln Glu Gln Val Gln Glu Gln Val
370 375 380
Gln Pro Lys Pro Leu Glu Ser
385 390
<210> 77
<211> 285
<212> PRT
<213> Artificial Sequence
<220>
<223> Tetranectin-apolipoprotein A-I
<400> 77
Lys Lys Ile Val Asn Ala Lys Lys Asp Val Val Asn Thr Lys Met Phe
1 5 10 15
Glu Glu Leu Lys Ser Arg Leu Asp Thr Leu Ala Gln Glu Val Ala Leu
20 25 30
Leu Lys Glu Gln Gln Ala Leu Gln Thr Val Asp Glu Pro Pro Gln Ser
35 40 45
Pro Trp Asp Arg Val Lys Asp Leu Ala Thr Val Tyr Val Asp Val Leu
50 55 60
Lys Asp Ser Gly Arg Asp Tyr Val Ser Gln Phe Glu Gly Ser Ala Leu
65 70 75 80
Gly Lys Gln Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser Val Thr
85 90 95
Ser Thr Phe Ser Lys Leu Arg Glu Gln Leu Gly Pro Val Thr Gln Glu
100 105 110
Phe Trp Asp Asn Leu Glu Lys Glu Thr Glu Gly Leu Arg Gln Glu Met
115 120 125
Ser Lys Asp Leu Glu Glu Val Lys Ala Lys Val Gln Pro Tyr Leu Asp
130 135 140
Asp Phe Gln Lys Lys Trp Gln Glu Glu Met Glu Leu Tyr Arg Gln Lys
145 150 155 160
Val Glu Pro Leu Arg Ala Glu Leu Gln Glu Gly Ala Arg Gln Lys Leu
165 170 175
His Glu Leu Gln Glu Lys Leu Ser Pro Leu Gly Glu Glu Met Arg Asp
180 185 190
Arg Ala Arg Ala His Val Asp Ala Leu Arg Thr His Leu Ala Pro Tyr
195 200 205
Ser Asp Glu Leu Arg Gln Arg Leu Ala Ala Arg Leu Glu Ala Leu Lys
210 215 220
Glu Asn Gly Gly Ala Arg Leu Ala Glu Tyr His Ala Lys Ala Thr Glu
225 230 235 240
His Leu Ser Thr Leu Ser Glu Lys Ala Lys Pro Ala Leu Glu Asp Leu
245 250 255
Arg Gln Gly Leu Leu Pro Val Leu Glu Ser Phe Lys Val Ser Phe Leu
260 265 270
Ser Ala Leu Glu Glu Tyr Thr Lys Lys Leu Asn Thr Gln
275 280 285
<210> 78
<211> 288
<212> PRT
<213> Artificial Sequence
<220>
<223> Tetrancetin Apolipoprotein A-I
<400> 78
Ile Val Asn Ala Lys Lys Asp Val Val Asn Thr Lys Met Phe Glu Glu
1 5 10 15
Leu Lys Ser Arg Leu Asp Thr Leu Ala Gln Glu Val Ala Leu Leu Lys
20 25 30
Glu Gln Gln Ala Leu Gln Thr Val Ser Leu Lys Gly Thr Asp Glu Pro
35 40 45
Pro Gln Ser Pro Trp Asp Arg Val Lys Asp Leu Ala Thr Val Tyr Val
50 55 60
Asp Val Leu Lys Asp Ser Gly Arg Asp Tyr Val Ser Gln Phe Glu Gly
65 70 75 80
Ser Ala Leu Gly Lys Gln Leu Asn Leu Lys Leu Leu Asp Asn Trp Asp
85 90 95
Ser Val Thr Ser Thr Phe Ser Lys Leu Arg Glu Gln Leu Gly Pro Val
100 105 110
Thr Gln Glu Phe Trp Asp Asn Leu Glu Lys Glu Thr Glu Gly Leu Arg
115 120 125
Gln Glu Met Ser Lys Asp Leu Glu Glu Val Lys Ala Lys Val Gln Pro
130 135 140
Tyr Leu Asp Asp Phe Gln Lys Lys Trp Gln Glu Glu Met Glu Leu Tyr
145 150 155 160
Arg Gln Lys Val Glu Pro Leu Arg Ala Glu Leu Gln Glu Gly Ala Arg
165 170 175
Gln Lys Leu His Glu Leu Gln Glu Lys Leu Ser Pro Leu Gly Glu Glu
180 185 190
Met Arg Asp Arg Ala Arg Ala His Val Asp Ala Leu Arg Thr His Leu
195 200 205
Ala Pro Tyr Ser Asp Glu Leu Arg Gln Arg Leu Ala Ala Arg Leu Glu
210 215 220
Ala Leu Lys Glu Asn Gly Gly Ala Arg Leu Ala Glu Tyr His Ala Lys
225 230 235 240
Ala Thr Glu His Leu Ser Thr Leu Ser Glu Lys Ala Lys Pro Ala Leu
245 250 255
Glu Asp Leu Arg Gln Gly Leu Leu Pro Val Leu Glu Ser Phe Lys Val
260 265 270
Ser Phe Leu Ser Ala Leu Glu Glu Tyr Thr Lys Lys Leu Asn Thr Gln
275 280 285
<210> 79
<211> 18
<212> PRT
<213> Artificial Sequence
<220>
<223> pro-polypeptide 5803
<400> 79
Met Arg Gly Ser His His His His His His Gly Ser Pro Arg Pro Pro
1 5 10 15
Thr Pro
<210> 80
<211> 27
<212> PRT
<213> Artificial Sequence
<220>
<223> plasmid 5816
<400> 80
Met Cys Asp Leu Pro Gln Thr His Ser Leu Gly Ser His His His His
1 5 10 15
His His Gly Ser Val Val Ala Pro Pro Ala Pro
20 25
<210> 81
<211> 146
<212> PRT
<213> Artificial Sequence
<220>
<223> plasmid 5820
<400> 81
Met Arg Gly Ser His His His His His His Gly Ser Ala Glu Ala Gly
1 5 10 15
Ile Thr Gly Thr Trp Tyr Asn Gln Leu Gly Ser Thr Phe Ile Val Thr
20 25 30
Ala Gly Ala Asp Gly Ala Leu Thr Gly Thr Tyr Glu Ser Ala Val Gly
35 40 45
Asn Ala Glu Ser Arg Tyr Val Leu Thr Gly Arg Tyr Asp Ser Ala Pro
50 55 60
Ala Thr Asp Gly Ser Gly Thr Ala Leu Gly Trp Thr Val Ala Trp Lys
65 70 75 80
Asn Asn Tyr Arg Asn Ala His Ser Ala Thr Thr Trp Ser Gly Gln Tyr
85 90 95
Val Gly Gly Ala Glu Ala Arg Ile Asn Thr Gln Trp Leu Leu Thr Ser
100 105 110
Gly Thr Thr Glu Ala Asn Ala Trp Lys Ser Thr Leu Val Gly His Asp
115 120 125
Thr Phe Thr Lys Val Lys Pro Ser Ala Ala Ser Val Val Ala Pro Pro
130 135 140
Ala Pro
145
<210> 82
<211> 23
<212> PRT
<213> Artificial Sequence
<220>
<223> plasmid 5805
<400> 82
Met Arg Gly Ser His His His His His His Ala His Phe Trp Gln Gln
1 5 10 15
Ala Pro Arg Pro Pro Thr Pro
20
<210> 83
<211> 139
<212> PRT
<213> Artificial Sequence
<220>
<223> plasmid 5819
<400> 83
Met Arg Gly Ser His His His His His His Thr Asp Pro Glu Phe Gln
1 5 10 15
Gln Gln Gln Gln Leu Leu Asp Val Val Lys Arg Gln Gln Glu Leu Leu
20 25 30
Arg Leu Thr Val Trp Gly Thr Lys Asn Leu Gln Ala Arg Val Thr Ala
35 40 45
Ile Glu Lys Tyr Leu Gln Asp Gln Ala Arg Leu Asn Ser Trp Gly Cys
50 55 60
Ala Phe Arg Gln Val Cys His Thr Thr Val Pro Trp Val Asn Asp Ser
65 70 75 80
Leu Ala Pro Asp Trp Asp Asn Met Thr Trp Gln Glu Trp Glu Lys Gln
85 90 95
Val Arg Tyr Leu Glu Ala Asn Ile Ser Lys Ser Leu Glu Gln Ala Gln
100 105 110
Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn Ser Trp
115 120 125
Asp Ile Arg Ser Val Val Ala Pro Pro Ala Pro
130 135
<210> 84
<211> 21
<212> PRT
<213> Artificial Sequence
<220>
<223> plasmid 5806
<400> 84
Met His His His His His His Lys Ala Lys Arg Phe Lys Lys His Pro
1 5 10 15
Arg Pro Pro Ala Pro
20
Claims (40)
- N-에서 C-말단 방향으로
제 1 다이펩타이드 GS,
아미노산 서열 태그,
효소 절단 부위에 바로 인접한 제 2 다이펩타이드 GS, 및
상기 효소 절단 부위
를 포함하는 프로-폴리펩타이드. - 제 1 항에 있어서,
제 1 다이펩타이드 GS에 대해 N-말단에 2 개 이상의 아미노산 잔기의 길이를 갖는 선도 아미노산 서열을 포함함을 특징으로 하는 프로-폴리펩타이드. - N-에서 C-말단 방향으로
제 1 항 또는 제 2 항에 따른 프로-폴리펩타이드, 및
관심 폴리펩타이드
를 포함하는 융합 폴리펩타이드. - 제 3 항에 있어서,
제 1 항 내지 제 3 항 중 어느 한 항에 따른 프로-폴리펩타이드의 N-말단의 아미노산이 유리 알파-아미노 기를 가짐을 특징으로 하는 융합 폴리펩타이드. - 제 1 항 내지 제 4 항 중 어느 한 항에 있어서,
아미노산 서열 태그가 서열번호 11 또는 서열번호 15의 아미노산 서열을 가짐을 특징으로 하는 폴리펩타이드. - 제 1 항 내지 제 5 항 중 어느 한 항에 있어서,
효소 절단 부위가 서열번호 33 또는 서열번호 34의 아미노산 서열을 가짐을 특징으로 하는 폴리펩타이드. - 제 2 항 내지 제 6 항 중 어느 한 항에 있어서,
제 1 다이펩타이드 GS에 대한 N-말단 선도 아미노산 서열이 서열번호 1 내지 8 중에서 선택된 아미노산 서열을 가짐을 특징으로 하는 폴리펩타이드. - 제 3 항 내지 제 7 항 중 어느 한 항에 있어서,
관심 폴리펩타이드가 항체 중쇄 또는 경쇄, 항체 단편, 단쇄 항체, 아포지방단백질, 아포지방단백질 변체, 아포지방단백질 융합물, 인터페론, 인터류킨, 인슐린, 조직 유형 플라스미노겐 활성화제 변체, 콜로니-자극 인자, 성장 호르몬, 및 골 형태발생 단백질 중에서 선택됨을 특징으로 하는 융합 폴리펩타이드. - 제 3 항 내지 제 7 항 중 어느 한 항에 있어서,
관심 폴리펩타이드가 서열번호 43 또는 서열번호 44 또는 서열번호 45의 아미노산 서열을 가짐을 특징으로 하는 융합 폴리펩타이드. - 관심 폴리펩타이드의 제조 방법으로서,
(a) N-에서 C-말단 방향으로
제 1 다이펩타이드 GS,
아미노산 서열 태그,
효소 절단 부위에 바로 인접한 제 2 다이펩타이드 GS,
상기 효소 절단 부위, 및
상기 관심 폴리펩타이드
를 포함하는 융합 폴리펩타이드를 암호화하는 핵산을 포함하는 세포를 제공하는 단계,
(b) 상기 세포를 배양하는 단계,
(c) 상기 세포 또는 배양 배지로부터 상기 융합 폴리펩타이드를 회수하는 단계,
(d) 상기 융합 폴리펩타이드를 정제하는 단계,
(e) 상기 융합 폴리펩타이드를 효소에 의해 절단하고 이에 의해 상기 관심 폴리펩타이드를 생성시키는 단계
를 포함하는 방법. - 제 10 항에 있어서,
융합 폴리펩타이드가 제 1 다이펩타이드 GS에 대해 N-말단에 2 개 이상의 아미노산 잔기의 길이를 갖는 선도 아미노산 서열을 포함함을 특징으로 하는 방법. - 제 11 항에 있어서,
제 1 다이펩타이드 GS에 대한 N-말단 선도 아미노산 서열이 서열번호 1 내지 8 중에서 선택된 아미노산 서열을 가짐을 특징으로 하는 방법. - 제 10 항 내지 제 12 항 중 어느 한 항에 있어서,
세포가 원핵생물 세포임을 특징으로 하는 방법. - 제 10 항 내지 제 13 항 중 어느 한 항에 있어서,
아미노산 서열 태그가 서열번호 11 또는 서열번호 15의 아미노산 서열을 가짐을 특징으로 하는 방법. - 제 10 항 내지 제 14 항 중 어느 한 항에 있어서,
효소 절단 부위가 서열번호 33 또는 서열번호 34의 아미노산 서열을 가짐을 특징으로 하는 방법. - 제 10 항 내지 제 15 항 중 어느 한 항에 있어서,
관심 폴리펩타이드가 항체 중쇄 또는 경쇄, 항체 단편, 단쇄 항체, 아포지방단백질, 아포지방단백질 변체, 아포지방단백질 융합물, 인터페론, 인터류킨, 인슐린, 조직 유형 플라스미노겐 활성화제 변체, 콜로니-자극 인자, 성장 호르몬, 및 골 형태발생 단백질 중에서 선택됨을 특징으로 하는 방법. - 제 10 항 내지 제 15 항 중 어느 한 항에 있어서,
폴리펩타이드가 서열번호 43 또는 서열번호 44 또는 서열번호 45의 아미노산 서열을 가짐을 특징으로 하는 방법. - 5'-에서 3'-방향으로
다이펩타이드 GS를 암호화하는 핵산,
아미노산 서열 태그를 암호화하는 핵산,
효소 절단 부위를 암호화하는 핵산에 바로 인접한 다이펩타이드 GS를 암호화하는 핵산, 및
상기 효소 절단 부위를 암호화하는 핵산
을 포함하는 핵산을 포함하는 키트. - 원핵생물 세포의 배양 방법으로서,
상기 원핵생물 세포를 글루코스, 효모 추출물, L-류신, L-프롤린, L-메티오닌, 티아민-HCl, 소포제를 포함하는 배지에서 배양하고,
상기 세포에 효모 추출물, 글리세롤, L-메티오닌, L-류신 및 L-프롤린을 포함하는 제 1 공급물 용액을 공급하고,
상기 세포에 L-프롤린을 포함하는 제 2 공급물 용액을 공급하고,
수산화 칼륨 용액 및 글루코스 용액을 pH 조절에 사용함
을 특징으로 하는 방법. - 폴리펩타이드의 제조 방법으로서,
상기 폴리펩타이드를 암호화하는 핵산을 포함하는 세포를 글루코스, 효모 추출물, L-류신, L-프롤린, L-메티오닌, 티아민-HCl, 소포제를 포함하는 배지에서 배양하고,
상기 세포에 효모 추출물, 글리세롤, L-메티오닌, L-류신 및 L-프롤린을 포함하는 제 1 공급물 용액을 공급하고,
상기 세포에 L-프롤린을 포함하는 제 2 공급물 용액을 공급하고,
수산화 칼륨 용액 및 글루코스 용액을 pH 조절에 사용함
을 특징으로 하고, 상기 폴리펩타이드를 상기 세포 또는 상기 배양 배지로부터 회수하고 이에 의해 폴리펩타이드를 생성시키는 방법. - 제 19 항 또는 제 20 항에 있어서,
제 1 공급물의 첨가를 578 ㎚에서 측정된 약 15의 광학 밀도에서 출발하고, 제 2 공급물의 첨가를 578 ㎚에서 측정된 약 50의 광학 밀도에서 출발하고, 폴리펩타이드의 발현을 578 ㎚에서 측정된 약 90의 광학 밀도에서 IPTG로 유도함을 특징으로 하는 방법. - 제 19 항 또는 제 21 항에 있어서,
배지가 약 8.85 g/ℓ의 글루코스, 약 63.5 g/ℓ의 효모 추출물, 약 2.2 g/ℓ의 NH4Cl, 약 1.95 g/ℓ의 L-류신, 약 2.9 g/ℓ의 L-프롤린, 약 0.75 g/ℓ의 L-메티오닌, 약 17.3 g/ℓ의 KH2PO4*3H2O, 약 2 g/ℓ의 MgSO4*7H2O, 약 25.8 ㎎/ℓ의 티아민-HCl, 약 1.0 ㎖/ℓ의 10% 소포제를 포함함을 특징으로 하는 방법. - 제 19 항 내지 제 22 항 중 어느 한 항에 있어서,
제 1 공급물 용액이 약 333 g/ℓ의 효모 추출물, 약 333 g/ℓ의 85% 글리세롤, 약 1.7 g/ℓ의 L-메티오닌, 및 약 5 g/ℓ의 L-류신 및 L-프롤린 각각을 포함함을 특징으로 하는 방법. - 제 19 항 내지 제 23 항 중 어느 한 항에 있어서,
제 2 공급물 용액이 약 600 g/ℓ의 L-프롤린을 포함함을 특징으로 하는 방법. - 제 19 항 내지 제 24 항 중 어느 한 항에 있어서,
pH 조절용 염기가 10%(w/v) KOH 용액이고 산이 75% 글루코스 용액임을 특징으로 하는 방법. - 제 19 항 내지 제 25 항 중 어느 한 항에 있어서,
배양이 약 25 ℃에서 수행됨을 특징으로 하는 방법. - 제 19 항 내지 제 26 항 중 어느 한 항에 있어서,
배양이 약 pH 6.5 내지 약 pH 6.9의 pH에서 수행됨을 특징으로 하는 방법. - 제 19 항 내지 제 27 항 중 어느 한 항에 있어서,
제 1 공급물이 70 g/h의 비율로 출발함을 특징으로 하는 방법. - 제 19 항 내지 제 28 항 중 어느 한 항에 있어서,
제 2 공급물이 10 ㎖/h의 비율로 출발함을 특징으로 하는 방법. - 제 19 항 내지 제 29 항 중 어느 한 항에 있어서,
용존 산소 값을 50% 이상으로 유지시킴을 특징으로 하는 방법. - 제 30 항에 있어서,
용존 산소 값을, 교반기 속도, 통기율, 및 공기압을 동시에 증가시킴으로써 50% 이상으로 유지시킴을 특징으로 하는 방법. - 제 19 항 내지 제 31 항 중 어느 한 항에 있어서,
교반기 속도가 약 500 rpm 내지 약 1500 rpm임을 특징으로 하는 방법. - 제 19 항 내지 제 32 항 중 어느 한 항에 있어서,
통기율이 약 10 ℓ/분 내지 약 20 ℓ/분임을 특징으로 하는 방법. - 제 19 항 내지 제 33 항 중 어느 한 항에 있어서,
공기압이 약 300 mbar 내지 약 500 mbar임을 특징으로 하는 방법. - 제 19 항 내지 제 34 항 중 어느 한 항에 있어서,
원핵생물 세포가 에스케리키아 콜라이 세포임을 특징으로 하는 방법. - 제 19 항 내지 제 35 항 중 어느 한 항에 있어서,
폴리펩타이드가 아포지방단백질 A1임을 특징으로 하는 방법. - 제 36 항에 있어서,
아포지방단백질 A1이 테트라넥틴-아포지방단백질 A1 전구체 단백질임을 특징으로 하는 방법. - 약 8.85 g/ℓ의 글루코스, 약 63.5 g/ℓ의 효모 추출물, 약 2.2 g/ℓ의 NH4Cl, 약 1.95 g/ℓ의 L-류신, 약 2.9 g/ℓ의 L-프롤린, 약 0.75 g/ℓ의 L-메티오닌, 약 17.3 g/ℓ의 KH2PO4*3H2O, 약 2 g/ℓ의 MgSO4*7H2O, 약 25.8 ㎎/ℓ의 티아민-HCl, 약 1.0 ㎖/ℓ의 10% 소포제를 포함하는 원핵생물 세포용 배양 배지.
- 제 38 항에 있어서,
약 333 g/ℓ의 효모 추출물, 약 333 g/ℓ의 85% 글리세롤, 약 1.7 g/ℓ의 L-메티오닌, 및 약 5 g/ℓ의 L-류신 및 L-프롤린 각각을 포함하는 제 1 공급물을 또한 포함함을 특징으로 하는 배양 배지. - 제 39 항에 있어서,
약 600 g/ℓ의 L-프롤린을 포함하는 제 2 공급물 용액을 또한 포함함을 특징으로 하는 배양 배지.
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EP10008996.0 | 2010-08-30 | ||
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EP10187663 | 2010-10-15 | ||
PCT/EP2011/064599 WO2012028523A2 (en) | 2010-08-30 | 2011-08-25 | Prokaryotic expression construct |
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US (1) | US8877895B2 (ko) |
EP (1) | EP2611921A2 (ko) |
JP (2) | JP2013535978A (ko) |
KR (1) | KR20130059404A (ko) |
CN (1) | CN103025875A (ko) |
CA (1) | CA2807431A1 (ko) |
MX (1) | MX2013001536A (ko) |
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MX2014001918A (es) | 2011-08-25 | 2014-04-14 | Hoffmann La Roche | Metodo de cromatografia de intercambio cationico y anionico. |
CA2838070A1 (en) | 2011-08-25 | 2013-02-28 | F. Hoffmann-La Roche Ag | Shortened tetranectin-apolipoprotein a-i fusion protein, a lipid particle containing it, and uses thereof |
ES2688268T3 (es) | 2011-12-05 | 2018-10-31 | Bio-Rad Laboratories, Inc. | Antígeno de gliadina desamidada recombinante |
GB201214746D0 (en) * | 2012-08-17 | 2012-10-03 | Cancer Rec Tech Ltd | Biomolecular complexes |
ES2688044T3 (es) * | 2013-02-22 | 2018-10-30 | F. Hoffmann-La Roche Ag | Uso de una cepa procariota con supresión de auxotrofias para aminoácidos para la producción recombinante de un polipéptido |
WO2015014829A1 (en) * | 2013-07-31 | 2015-02-05 | F. Hoffmann-La Roche Ag | Method for the recombinant production of a polypeptide in prokaryotic cells |
CN113025599B (zh) * | 2021-04-02 | 2023-09-12 | 重庆科润生物医药研发有限公司 | 一种重组溶组织梭菌i型胶原酶及其制备方法和应用 |
JP2023140872A (ja) * | 2022-03-23 | 2023-10-05 | 藤森工業株式会社 | 細胞培養装置および細胞培養方法 |
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NZ236819A (en) * | 1990-02-03 | 1993-07-27 | Max Planck Gesellschaft | Enzymatic cleavage of fusion proteins; fusion proteins; recombinant dna and pharmaceutical compositions |
JPH08506801A (ja) | 1992-11-20 | 1996-07-23 | アイシス・イノベーション・リミテッド | Cd44エキソン6に対応するペプチド、そのペプチドに特異的な抗体、および、腫瘍診断にそれらの抗体を使用する方法 |
DK0710248T3 (da) * | 1993-07-20 | 2000-04-10 | Roche Diagnostics Gmbh | Melanom-inhiberende protein |
US5789655A (en) * | 1994-05-13 | 1998-08-04 | The Regents Of The University Of California | Transgenic animals expressing artificial epitope-tagged proteins |
EP1173191A4 (en) * | 1997-05-13 | 2004-12-01 | Univ California | NOVEL ANTI-ANGIOGENIC PEPTIDE AGENTS, USE OF THE SAME FOR THERAPY AND DIAGNOSIS |
CA2304254C (en) * | 1997-06-11 | 2012-05-22 | Hans Christian Thogersen | Trimerising module |
US6291245B1 (en) | 1998-07-15 | 2001-09-18 | Roche Diagnostics Gmbh | Host-vector system |
EP0972838B1 (en) | 1998-07-15 | 2004-09-15 | Roche Diagnostics GmbH | Escherichia coli host/vector system based on antibiotic-free selection by complementation of an auxotrophy |
EP2343317A1 (en) * | 2000-11-10 | 2011-07-13 | F. Hoffmann-La Roche Ltd. | Apolipoprotein analogues |
CA2443365C (en) | 2002-11-19 | 2010-01-12 | F. Hoffmann-La Roche Ag | Methods for the recombinant production of antifusogenic peptides |
ATE312939T1 (de) * | 2003-06-12 | 2005-12-15 | Verfahren zur rekombinanten herstellung von polypeptiden | |
CA2609613A1 (en) * | 2005-05-26 | 2006-11-30 | Schering Corporation | Interferon-igg fusion |
EP2059530B1 (en) * | 2006-08-31 | 2012-08-29 | F.Hoffmann-La Roche Ag | Method for the production of insulin-like growth factor-i |
US20100062984A1 (en) * | 2007-01-25 | 2010-03-11 | Rajiv Kumar | Fgf-23 polypeptides |
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- 2011-08-25 MX MX2013001536A patent/MX2013001536A/es not_active Application Discontinuation
- 2011-08-25 WO PCT/EP2011/064599 patent/WO2012028523A2/en active Application Filing
- 2011-08-25 KR KR1020137005002A patent/KR20130059404A/ko not_active Application Discontinuation
- 2011-08-25 US US13/217,537 patent/US8877895B2/en active Active
- 2011-08-25 JP JP2013525304A patent/JP2013535978A/ja active Pending
- 2011-08-25 CA CA2807431A patent/CA2807431A1/en not_active Abandoned
- 2011-08-25 RU RU2013111677/10A patent/RU2013111677A/ru not_active Application Discontinuation
- 2011-08-25 CN CN2011800365946A patent/CN103025875A/zh active Pending
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EP2611921A2 (en) | 2013-07-10 |
US8877895B2 (en) | 2014-11-04 |
WO2012028523A2 (en) | 2012-03-08 |
RU2013111677A (ru) | 2014-10-10 |
CN103025875A (zh) | 2013-04-03 |
MX2013001536A (es) | 2013-03-18 |
WO2012028523A3 (en) | 2012-04-26 |
US20120214200A1 (en) | 2012-08-23 |
CA2807431A1 (en) | 2012-03-08 |
JP2013535978A (ja) | 2013-09-19 |
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