KR101700974B1 - 친화성 태그가 결합된 융합 콜라게나제 및 그의 제조방법 - Google Patents
친화성 태그가 결합된 융합 콜라게나제 및 그의 제조방법 Download PDFInfo
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- KR101700974B1 KR101700974B1 KR1020117012485A KR20117012485A KR101700974B1 KR 101700974 B1 KR101700974 B1 KR 101700974B1 KR 1020117012485 A KR1020117012485 A KR 1020117012485A KR 20117012485 A KR20117012485 A KR 20117012485A KR 101700974 B1 KR101700974 B1 KR 101700974B1
- Authority
- KR
- South Korea
- Prior art keywords
- lys
- asn
- asp
- ser
- gly
- Prior art date
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Abstract
콜라게나제의 카르복실 말단에 친화성 태그을 부가시킨 융합 콜라게나제를 조환 단백질로 발현시켰다. 얻어진 융합 콜라게나제를 친화성 크로마토그래피로 정제함으로써, 콜라겐 결합 부위를 가진 콜라게나제를 선택적으로 회수할 수가 있음을 알아내었다.
Description
본 발명은 췌장 등의 장기로부터 췌도(膵島) 등의 세포(덩어리)를 단리할 때에 사용되는 콜라게나제에 관한 것이다.
당뇨병의 완치(根治) 요법으로서, 프로테아제로 처리한 췌장으로부터 단리되는 췌도(인슐린 생산세포)를 당뇨병 환자의 문맥(門脈)에 점적(点滴)으로 이식하는 췌도이식이 알려져 있다. 본 이식법은 이식할 때 환자의 개복 수술 필요 없기 때문에 안전하고 간편한 당뇨병의 완치 요법으로서 근래에 들어 주목되고 있다.
췌장으로부터의 췌도의 분리는 췌장을 콜라게나제와 중성 금속 프로테아제로 처리함으로써 실시되는데, 이와 같은 목적으로 사용되는 콜라게나제로는 클로스트리디움·히스트리티캄 유래인 것이 특히 유효하다 (비특허문헌 1, 2).
클로스트리디움·히스트리티캄 유래의 콜라게나제는 기질 특이성이 다른 2종류의 효소인, 콜라게나제 G 및 콜라게나제 H로 이루어지는 것이 알려져 있다(비특허문헌 1, 2). 콜라게나제 G 및 콜라게나제 H를 코드하는 유전자는 이미 단리되어 있고, 양 콜라게나제 모두 아미노기 말단 측의 촉매 부위와 카르복실 말단 측의 콜라겐 결합 부위(이하, 「CBD」라고 칭함)로 이루어진 다중 도메인 효소인 것이 분명해져 있다 (비특허문헌 1, 2).
그러나 콜라게나제에는, 클로스트리디움·히스트리티캄에 의해 생산되는 경우에 발현된 콜라게나제의 일부가 분해되어서(비특허문헌 2), 이들 분해된 콜라게나제가 혼입되어 있는 콜라게나제로 췌장을 처리하면, 분리된 췌도의 질이 저하된다고 하는 문제가 있었다. 따라서 분해된 콜라게나제를 가능한 한 제거한 콜라게나제를 취득하고, 이와 같은 콜라게나제로 췌장을 처리하는 것이 췌도의 분리에 있어 요망되고 있다.
그러나 분해되어 있지 않은 콜라게나제와, 분해된 콜라게나제는, 그들의 물리화학적 성질이 비슷하기 때문에, 이온교환 크로마토그래피나 소수(疏水) 크로마토그래피 등의 방법으로 이들 콜라게나제를 분리하기가 곤란하였다.
이와 같은 배경 중, 클로스트리디움·히스트리티캄 유래의 콜라게나제에 있어서, 분해되어 있지 않은 콜라게나제를 선택적으로 회수하는 콜라게나제의 조제법 이 소망되고 있었다.
한편, 클로스트리디움·히스트리티캄 유래의 콜라게나제를, 대장균 등을 숙주로 조환 단백질로서 발현시킨 경우에서 콜라게나제의 분해에 대해서는 아직도 보고되고 있지 않다.
비특허문헌 1 : Yoshihara, K. et.al. Journal of Bacteriology. (1994), 176, 6489-6496
비특허문헌 2 : Matsushita, O. et.al. Journal of Bacteriology. (1999), 181, 923-933
본 발명에서는 클로스트리디움·히스트리티캄 유래의 콜라게나제 중에서, 분해된 콜라게나제를 제거하고 분해되어 있지 않은 콜라게나제를 선택적으로 회수하는 것을 과제로 한다.
본 발명자들은 클로스트리디움·히스트리티캄 유래의 콜라게나제에서, 그들의 카르복실 말단에 친화성 태그(attinity tag)을 결합시킨 융합 콜라게나제를 조환 단백질로서 발현시켰다. 클로스트리디움·히스트리티캄 유래의 콜라게나제를, 대장균 등을 숙주로 조환 단백질로서 발현시켰을 경우, 이 조환 단백질이 숙주 내의 프로테아제에 의한 작용으로 분해되는지 여부, 또 분해된다면 어떻게 분해되는 것인지는 예측할 수가 없었다. 그러나 본 발명자들은 숙주에서 발현시킨 융합단백질을 친화성 컬럼으로 정제할 때, 우연히도 분해된 콜라게나제가 제거되어 콜라게나제 활성을 가진 단일의 콜라게나제가 선택적으로 회수되는 것을 알아내었다. 이는 숙주 내에서 발현시켜진 클로스트리디움·히스트리티캄 유래의 콜라게나제의 분해가 융합된 친화성 태그의 근방에 있는 CBD에서 생긴 것이어서, CBD의 분해에 수반해서 친화성 태그가 콜라게나제에서 분리되고, 친화성 크로마토그래피에 의한 정제 단계에서 친화성 컬럼에 분해 콜라게나제가 흡착되지 않고, 분해되어 있지 않은 콜라게나제만 친화성 컬럼에 흡착된 것에 기한 것으로 생각된다.
즉, 본 발명자들은 콜라게나제와 친화성 태그를 특정한 배치로 결합시키는 것에 의하면, 친화성 정제의 과정에서 숙주 내에서 분해된 콜라게나제를 흡착시키지 않고, 콜라게나제 활성을 가진 단일의 콜라게나제를 선택적으로 회수할 수 있음을 알아내어 본 발명을 완성하기에 이르렀다.
본 발명은 이하의 발명에 관한 것이다.
<1> 콜라게나제에 직접 또는 간접적으로 친화성 태그가 결합된 융합 콜라게나제로서, 숙주 내에서 발현시켜진 당해 융합 콜라게나제가 당해 숙주의 작용에 의해 분해된 경우에 콜라게나제 활성을 가진 단편과 친화성 태그가 분리되도록, 콜라게나제와 친화성 태그가 결합되어 있는 융합 콜라게나제.
<2> 콜라게나제의 카르복실 말단에 직접 또는 간접적으로 친화성 태그가 결합된, <1>에 기재된 융합 콜라게나제.
<3> 친화성 태그가 2개 이상의 연속하는 히스티딘 잔기인, <2>에 기재된 융합 콜라게나제.
<4> 콜라게나제가 클로스트리디움·히스트리티캄에 유래하는, <1>에 기재된 융합 콜라게나제.
<5> 콜라게나제의 아미노산 서열이 이하의 (i), (ⅱ), (ⅲ) 및 (ⅳ)로부터 선택되는, <1>에 기재된 융합 콜라게나제:
(i) 서열번호:1 또는 2에 기재된 -110번에서 1008번까지의 아미노산 서열의 전부 또는 일부를 포함해서 이루어진 콜라게나제;
(ⅱ) 서열번호:1 또는 2에 기재된 -110번에서 1008번까지의 아미노산 서열에서, 1 또는 복수 개의 아미노산이 결실, 치환, 삽입 또는 부가된 아미노산 서열을 포함해서 이루어진 콜라게나제;
(ⅲ) 서열번호:1 또는 2에 기재된 -110번에서 1008번까지의 아미노산 서열과 70% 이상의 상동성(相同性)을 가진 아미노산 서열을 포함해서 이루어진 콜라게나제;
(ⅳ) (i)에서부터 (ⅲ)에 기재된 콜라게나제에서, 서열번호:1 또는 2에 기재된 -1번에서 -110번까지의 아미노산 서열의 전부 또는 일부가 제거된 콜라게나제.
<6> 서열번호:3에 기재된 -110번에서 1021번까지의 아미노산 서열의 전부 또는 일부로 이루어지는 <5>에 기재된 융합 콜라게나제.
<7> 서열번호:3에 기재된 -1번에서 -110번까지의 아미노산 서열의 전부 또는 일부가 제거된 <6>에 기재된 융합 콜라게나제.
<8> 콜라게나제의 아미노산 서열이 이하의 (i), (ii), (iii) 및 (iv)로부터 선택되는 <1>에 기재된 융합 콜라게나제:
(i) 서열번호:5 또는 6에 기재된 -40번에서 981번까지의 아미노산 서열의 전부 또는 일부를 포함해서 이루어지는 콜라게나제;
(ii) 서열번호:5 또는 6에 기재된 -40번에서 981번까지의 아미노산 서열에서, 1 또는 복수 개의 아미노산이 결실, 치환, 삽입 또는 부가된 아미노산 서열을 포함해서 이루어지는 콜라게나제;
(iii) 서열번호:5 또는 6에 기재된 -40번에서 981번까지의 아미노산 서열과 70% 이상의 상동성을 가진 아미노산 서열을 포함해서 이루어진 콜라게나제;
(iv) (i)에서부터 (iii)에 기재된 콜라게나제에서, 서열번호:5 또는 6에 기재된 -1번에서 -40번까지의 아미노산 서열의 전부 또는 일부가 제거된 콜라게나제.
<9> 서열번호:7에 기재된 -40번에서 994번까지의 아미노산 서열의 전부 또는 일부로 이루어지는 <8>에 기재된 융합 콜라게나제.
<10> 서열번호:7에 기재된 -1에서 -40번까지의 아미노산 서열의 전부 또는 일부가 제거된 <9>에 기재된 융합 콜라게나제.
<11> <1>에서부터 <10> 중의 어느 한 항에 기재된 융합 콜라게나제를 코드하는 DNA.
<12> 서열번호:4에 기재된 1번에서 3396번까지의 염기서열로 이루어지는 DNA.
<13> 서열번호:8에 기재된 1번에서 3105번까지의 염기서열로 이루어지는 DNA.
<14> <11>에서부터 <13> 중의 어느 한 항에 기재된 DNA를 포함해서 이루어지는 발현 벡터.
<15> <11>에서부터 <13> 중 어느 한 항에 기재된 DNA, 또는 <14>에 기재된 발현 벡터에 의해 형질전환된 숙주세포.
<16> 숙주세포가 대장균인 <15>에 기재된 숙주세포.
<17> <15> 또는 <16>에 기재된 숙주세포를 배양하고 얻어지는 배양물을, 친화성 태그에 대응한 친화성 크로마토그래피로 정제함으로써, 콜라겐 결합 부위를 가진 융합 콜라게나제를 선택적으로 채취하는 것을 특징으로 하는 융합 콜라게나제의 제조방법.
<18> <17>에 기재된 방법으로 제조된 융합 콜라게나제.
본 발명에 의해, 클로스트리디움·히스트리티캄에 유래하는 콜라게나제에 친화성 태그가 결합된 융합 콜라게나제로서, 숙주 내에서 발현시켜진 당해 융합 콜라게나제가 당해 숙주의 작용에 의해 분해된 경우에 콜라게나제 활성을 가진 단편과 친화성 태그가 분리되도록, 콜라게나제와 친화성 태그가 결합되어 있는 융합 콜라게나제가 제공된다. 또한 당해 융합 콜라게나제를 조환 단백질로서 효율적으로 생산하기 위해 필요한 DNA 및 당해 융합 콜라게나제를 조환 단백질로서 발현하는 숙주세포가 제공된다. 그리고 당해 융합 콜라게나제를 발현하는 숙주세포를 배양하고 얻어지는 배양액으로부터 CBD의 일부 또는 전부가 분해된 콜라게나제를 제거해서, CBD를 가진 단일의 융합 콜라게나제를 선택적으로 회수하게 하는 방법이 제공된다. 본 발명에 의해 CBD를 가진 융합 콜라게나제를 효율적으로 생산하는 것이 가능해지게 된다.
도 1은 플라스미드 pColG의 구조를 나타낸 도면이다. 도면 중의 기호의 의미는 다음과 같다(도면 중의 이탤릭체는 밑줄로 나타내었다). colG:콜라게나제 G유전자, PlacZ:lacZ 프로모터, Amp r :암피실린 내성 유전자.
도 2는 플라스미드 pColG-His의 구조를 나타낸 도면이다. 도면 중의 기호의 의미는, 다음과 같다(도면 중의 이탤릭체는 밑줄로 나타내었다). colG:콜라게나제 G유전자, PlacZ:lacZ 프로모터, Amp r :암피실린 내성 유전자, MCS:다중 클로닝 부위, 6XHis:히스티딘 태그.
도 3은 융합 콜라게나제 G를 발현시킨 대장균의 추출액에 대해, 활성 염색을 실시한 결과를 나타내는 전기영동사진이다.
도 4는 친화성 크로마토그래피에 제공된 융합 콜라게나제 G용액에 대해, 활성 염색을 실시한 결과를 나타내는 전기영동사진이다.
도 5는 플라스미드 pColH의 구조를 나타낸 도면이다. 도면 중의 기호의 의미는 다음과 같다(도면 중의 이탤릭체는 밑줄로 나타내었다). colH:콜라게나제 H유전자, PlacZ:lacZ 프로모터, Amp r :암피실린 내성 유전자.
도 6은 플라스미드 pColH-His의 구조를 나타낸 도면이다. 도면 중의 기호의 의미는 다음과 같다(도면 중의 이탤릭체는 밑줄로 나타내었다). colH:콜라게나제 H유전자, PlacZ:lacZ 프로모터, Amp r :암피실린 내성 유전자, MCS: 다중 클로닝 부위, 6XHis:히스티딘 태그.
도 7은 융합 콜라게나제 H를 발현시킨 대장균의 추출액을에 대해, 활성 염색을 실시한 결과를 나타내는 전기영동사진이다.
도 8은 친화성 크로마토그래피에 제공한 융합 콜라게나제 H용액에 대해, 활성 염색을 실시한 결과를 나타내는 전기영동사진이다.
도 2는 플라스미드 pColG-His의 구조를 나타낸 도면이다. 도면 중의 기호의 의미는, 다음과 같다(도면 중의 이탤릭체는 밑줄로 나타내었다). colG:콜라게나제 G유전자, PlacZ:lacZ 프로모터, Amp r :암피실린 내성 유전자, MCS:다중 클로닝 부위, 6XHis:히스티딘 태그.
도 3은 융합 콜라게나제 G를 발현시킨 대장균의 추출액에 대해, 활성 염색을 실시한 결과를 나타내는 전기영동사진이다.
도 4는 친화성 크로마토그래피에 제공된 융합 콜라게나제 G용액에 대해, 활성 염색을 실시한 결과를 나타내는 전기영동사진이다.
도 5는 플라스미드 pColH의 구조를 나타낸 도면이다. 도면 중의 기호의 의미는 다음과 같다(도면 중의 이탤릭체는 밑줄로 나타내었다). colH:콜라게나제 H유전자, PlacZ:lacZ 프로모터, Amp r :암피실린 내성 유전자.
도 6은 플라스미드 pColH-His의 구조를 나타낸 도면이다. 도면 중의 기호의 의미는 다음과 같다(도면 중의 이탤릭체는 밑줄로 나타내었다). colH:콜라게나제 H유전자, PlacZ:lacZ 프로모터, Amp r :암피실린 내성 유전자, MCS: 다중 클로닝 부위, 6XHis:히스티딘 태그.
도 7은 융합 콜라게나제 H를 발현시킨 대장균의 추출액을에 대해, 활성 염색을 실시한 결과를 나타내는 전기영동사진이다.
도 8은 친화성 크로마토그래피에 제공한 융합 콜라게나제 H용액에 대해, 활성 염색을 실시한 결과를 나타내는 전기영동사진이다.
(융합
콜라게나제
)
본 발명에서 융합 콜라게나제라 함은 콜라게나제에 직접 또는 간접적으로 친화성 태그가 결합된 단백질로서, 숙주 내에서 발현시켜진 당해 융합 콜라게나제가 당해 숙주의 작용에 의해 분해된 경우에 당해 융합 콜라게나제에서의 콜라게나제 활성을 가진 단편과 친화성 태그가 분리되도록, 콜라게나제와 친화성 태그가 결합되어 있는 융합 콜라게나제를 가리킨다. 이와 같은 콜라게나제의 친화성 태그로의 결합 양식은, 바람직하기는 콜라게나제의 CBD로의 결합이고, 가장 바람직하기는 CBD의 카르복시 말단(즉, 콜라게나제의 카르복실 말단)에의 결합이다. 본 발명에서 「CBD」란, 콜라게나제 G에서의 세그먼트(segment) 3a 및 3b의 영역(서열번호:1 및 2의 776 위치 ~ 카르복시 말단), 및 콜라게나제 H에서의 세그먼트 3의 영역(서열번호:5의 864 위치 ~ 카르복시 말단)을 의미한다(비특허문헌 2).
본 발명에서 콜라게나제로는 중성 금속 프로테아제와 함께 처리함으로써, 췌장으로부터 췌도(膵島)를 단리할 수 있다면, 어떤 콜라게나제도 이용할 수 있는바, 특히 클로스트리디움·히스트리티캄 유래의 콜라게나제의 이용이 바람직하다. 클로스트리디움·히스트리티캄 유래의 콜라게나제로는, 어떤 콜라게나제도 이용할 수 있지만, 특히 서열번호 1 또는 2에 기재된 콜라게나제 G나 서열번호 5 또는 6에 기재된 콜라게나제 H를 이용하는 것이 바람직하다. 또한 이들 콜라게나제는 시그널 서열의 전부 또는 일부가 제거된 아미노산 서열로 이루어진 것이어도 상관이 없다.
여기서 콜라게나제 G의 아미노산 서열은 콜라게나제 활성 및 콜라겐으로의 결합성이 유지되어 있다면, (i) 서열번호:1 또는 2에 기재된 -110번에서 1008번까지의 아미노산 서열의 전부 또는 일부를 포함해서 이루어진 콜라게나제; (ii) 서열번호:1 또는 2에 기재된 -110번에서 1008번까지의 아미노산 서열에서 1 또는 복수 개의 아미노산이 결실, 치환, 삽입 또는 부가된 아미노산 서열을 포함해서 이루어진 콜라게나제; (iii) 서열번호:1 또는 2에 기재된 -110번에서 1008번까지의 아미노산 서열과 70% 이상의 상동성을 가진 아미노산 서열을 포함해서 이루어진 콜라게나제; (ⅳ) (i)에서부터 (iii)에 기재된 콜라게나제에서 서열번호:1 또는 2에 기재된 -1번에서-110번까지의 아미노산 서열로 이루어진 시그널 서열의 전부 또는 일부가 제거된 콜라게나제 중의 어느 것이어도 상관이 없다.
마찬가지로 콜라게나제 H의 아미노산 서열은 콜라게나제 활성 및 콜라겐으로의 결합성이 유지되어 있다면, (i) 서열번호:5 또는 6에 기재된 -40번에서 981번까지의 아미노산 서열의 전부 또는 일부를 포함해서 이루어진 콜라게나제; (ii) 서열번호:5 또는 6에 기재된 -40번에서 981번까지의 아미노산 서열에서 1 또는 복수 개의 아미노산이 결실, 치환, 삽입 또는 부가된 아미노산 서열을 포함해서 이루어진 콜라게나제; (iii) 서열번호:5 또는 6에 기재된 -40번에서 981번까지의 아미노산 서열과 70% 이상의 상동성을 가진 아미노산 서열을 포함해서 이루어진 콜라게나제; (iv) (i)에서부터 (iii)에 기재된 콜라게나제에서 서열번호:5 또는 6에 기재된 -1번에서 -40번까지의 아미노산 서열로 이루어진 시그널 서열의 전부 또는 일부가 제거된 콜라게나제 중 어느 것이어도 상관이 없다.
여기서 「아미노산 서열에서 1 또는 복수 개의 아미노산이 결실, 치환, 삽입 또는 부가된 아미노산 서열」이란, 부위 특이적 돌연변이 유발법 등의 주지된 방법으로, 또는 천연에서 생길 수 있는 정도의 복수 개 수의 아미노산의 치환 등에 의해 변이(改變)가 이루어진 것을 의미한다. 아미노산의 변이의 개수는, 바람직하기는 1 ~ 50개, 보다 바람직하기는 1 ~ 30개, 더 바람직하기는 1 ~ 10개, 보다 더 바람직하기는 1 ~ 5개, 가장 바람직하기는 1 ~ 2개이다. 변이 아미노산 서열의 예는, 바람직하기는, 그 아미노산이 1 또는 복수 개(바람직하기는, 1 내지 수 개 또는 1, 2, 3, 또는 4개)의 보존적 치환을 가진 아미노산 서열일 수가 있다. 여기서 「보존적 치환」이란, 1 또는 복수 개의 아미노산 잔기를, 별개의 화학적으로 유사한 아미노산 잔기로 치환하는 것을 의미한다. 예컨대, 어떤 소수성 잔기를 별개의 소수성 잔기에 의해 치환하는 경우, 어떤 극성 잔기를 같은 전하(電荷)를 가진 별개의 극성 잔기에 의해 치환하는 경우 등을 들 수 있다. 이와 같은 치환을 실행할 수가 있는 기능적으로 유사한 아미노산은 아미노산마다 당해 기술분야에 있어서 공지된 것이다. 구체적인 예를 들자면, 비극성(소수성) 아미노산으로는 알라닌, 바린, 이소로이신, 로이신, 프롤린, 트립토판, 페닐알라닌, 메티오닌 등을 들 수 있다. 극성(중성) 아미노산으로는 글리신, 세린, 트레오닌, 티로신, 글루타민, 아스파라긴, 시스테인 등을 들 수 있다. 양전하를 가진(염기성) 아미노산으로는 알기닌, 히스티딘, 라이신 등을 들 수 있다. 또 음전하를 가진(산성) 아미노산으로는 아스파라긴산, 글루타민산 등을 들 수 있다.
또, 「70% 이상의 상동성을 가진 아미노산 서열」은 바람직하기는 80% 이상, 보다 바람직하기는 85% 이상, 더 바람직하기는 90% 이상, 보다 더 바람직하기는 95% 이상, 특히 바람직하기는 98% 이상, 그리고 가장 바람직하기는 99% 이상의 동일성을 가진 아미노산 서열일 수가 있다. 염기서열 또는 아미노산 서열에 대한 「상동성」은, 비교되는 서열 사이에서 각각의 서열을 구성하는 염기 또는 아미노산 잔기의 일치의 정도를 의미한다. 본 명세서에서 나타낸 「상동성」의 수치는 모두, 당업자에게 공지된 상동성 검색 프로그램을 이용해서 산출되는 수치이면 좋은바, 예컨대 FASTA, BLAST 등에서 디폴트(초기 설정)의 파라미터를 이용함으로써 용이하게 산출할 수가 있다.
본 발명에서 콜라게나제에 직접 또는 간접적으로 융합되는 친화성 태그는 어떤 종류의 담체와 선택적으로 결합될 수 있다면, 어떤 친화성 태그도 이용될 수 있다. 예컨대, 일본국 특허 제2686090호에 기재된 니켈 킬레이트 컬럼에 선택적으로 결합되는 2개 이상의 연속하는 히스티딘 잔기로 된 히스티딘 태그, 불용성 셀룰로오스에 선택적으로 결합하는 셀룰로오스 결합 부위, 말토스 결합 수지에 선택적으로 결합하는 말토스 결합 부위 등을 이용할 수 있는바, 특히 분자량이 작은 히스티딘 태그의 이용이 요망된다.
본 발명에서 친화성 태그는 콜라게나제에 직접 또는 간접적으로 결합시킨다. 여기서 콜라게나제와 친화성 태그를 간접적으로 결합시키는 경우에, 양자 사이에 개재되는 아미노산의 서열은 융합 콜라게나제의 활성 및 콜라겐으로의 결합성을 크게 저해하지 않는다면, 어떤 서열이어도 상관이 없다.
상기의 요건을 만족시키는 융합 콜라게나제로는 예컨대 콜라게나제 G의 카르복실 말단에 히스티딘 태그를 결합시킨 서열번호:3의 아미노산 서열의 전부로 이루어진 융합 콜라게나제나 콜라게나제 H의 카르복실 말단에 히스티딘 태그를 결합시킨 서열번호:7의 아미노산 서열의 전부로 이루어진 융합 콜라게나제를 들 수 있다. 또, 콜라게나제 활성, 콜라겐으로의 결합성, 및 친화성 태그로의 결합성이 유지되어 있는 한, 그들의 일부로 되는 융합 콜라게나제도 될 수가 있다.
(융합
콜라게나제의
아미노산 서열을
코드하는
DNA
)
본 발명에서 융합 콜라게나제를 코드하는 DNA는 상기의 융합 콜라게나제의 아미노 서열을 코드하는 것이라면, 어떤 염기서열로 이루어진 DNA이더라도 상관이 없다.
본 발명의 융합 콜라게나제를 코드하는 DNA는 인공적으로 화학합성을 함으로써 얻을 수가 있다. 또, 융합 콜라게나제를 코드하는 DNA는 콜라게나제를 코드하는 DNA와 친화성 태그를 코드하는 DNA를 각각 따로 구축하고 그들을 연결함으로써 얻을 수도 있다. 이때 콜라게나제 유전자는 당해 유전자의 서열을 기초로 해서 합성된 프라이머를 사용해서, 게놈 DNA, cDNA, 플라스미드 등 당해 유전자가 포함하는 DNA를 주형으로 한 PCR에 의해 증폭할 수가 있다. 예컨대, 클로스트리디움·히스트리티캄 유래의 콜라게나제 G 또는 콜라게나제 H의 경우에는 비특허문헌 1에 기재된 콜라게나제 G유전자 또는 비특허문헌 2에 기재된 콜라게나제 H 유전자의 서열의 5' 측 말단, 3' 측 말단의 서열을 기초로 해서 설계된 프라이머를 이용해서, 클로스트리디움·히스트리티캄 유래의 게놈 DNA를 주형으로 한 PCR에 의해 증폭할 수가 있다. 또, 친화성 태그를 코드하는 DNA에서는 친화성 태그를 코드하는 유전자가 포함된 게놈 DNA, cDNA, 플라스미드 등을 주형으로 한 PCR에 의해 증폭할 수가 있다. 예컨대, 히스티딘 태그를 코드하는 DNA인 경우, 시판되고 있는 벡터인 pET-24a(+)를 주형으로 한 PCR에 의해 증폭할 수가 있다.
상기의 요건을 만족시키는 DNA로는, 예컨대 콜라게나제 G의 카르복실 말단에 히스티딘 태그를 결합시킨 융합 콜라게나제를 코드하는 서열번호:4의 염기서열의 전부 또는 일부로 이루어진 DNA를 들 수 있다. 또, 콜라게나제 H의 카르복실 말단에 히스티딘 태그를 결합시킨 서열번호:8의 염기서열의 전부 또는 일부로 이루어진 DNA를 들 수 있다.
(발현 벡터 및, 발현 벡터에 의해 형질전환된 숙주세포)
본 발명에서는 상기의 융합 콜라게나제의 아미노산 서열을 코드하는 DNA를 숙주세포 내에서 복제 가능하고, 또 그 DNA 서열이 코드하는 단백질을 발현 가능한 상태로 포함해서 이루어진 발현 벡터가 제공된다. 본 발현벡터는 자기 복제 벡터, 즉 염색체 외의 독립체로서 존재하고, 그의 복제가 염색체의 복제에 의존하지 않는, 예컨대 플라스미드를 기본으로 구축할 수가 있다. 또, 본 발현벡터는 숙주세포에 도입되었을 때, 그 숙주세포의 게놈 중에 조립되어, 그것이 조립된 염색체와 함께 복제되는 것이어도 좋다. 본 발명에 의한 벡터 구축의 순서 및 방법은 유전자공학 분야에서 관용되어 있는 것을 이용할 수가 있다.
본 발명에 의한 발현 벡터는 이를 실제로 숙주세포에 도입해서 융합 콜라게나제를 발현시키기 위해, 상기의 융합 콜라게나제의 아미노산 서열을 코드하는 DNA 외에, 그 발현을 제어하는 DNA 서열이나 형질전환된 숙주세포를 선택하기 위한 유전자 마커 등을 포함하고 있는 것이 바람직하다. 발현을 제어하는 DNA 서열로는 프로모터, 터미네이터, 및 시그널 펩티드를 코드하는 DNA 서열 등이 이에 포함된다. 프로모터는 숙주세포에서 전사 활성을 나타낸 것이라면 특히 한정되지 않고, 숙주세포와 동종 또는 이종의 어떤 단백질을 코드하는 유전자의 발현을 제어하는 DNA 서열로부터 얻을 수가 있다. 또, 시그널 펩티드는 숙주세포에서 단백질의 분비에 기여하는 것이라면 특히 한정되지 않고, 숙주세포와 동종 또는 이종의 어떤 단백질을 코드하는 유전자로부터 유도되는 DNA 서열로부터 얻을 수가 있다. 또, 본 발명에서의 유전자 마커는 형질전환체의 선택 방법에 대응해서 적의 선택되어도 좋은바, 예컨대 약제 내성을 코드하는 유전자나 영양 요구성을 상보(相補)하는 유전자를 이용할 수 있다.
또 본 발명에 의하면, 이 발현 벡터에 의해 전질변환된 숙주세포가 제공된다. 이 숙주-벡터계(系)는 특히 한정되지 않고, 예컨대 대장균, 방선균, 효모, 사상균, 동물세포 등을 이용한 계(系) 등을 이용할 수 있으나, 특히 대장균을 숙주로 이용하는 것이 바람직하다.
또, 이들 발현 벡터에 의한 숙주세포의 형질전환도 이 분야에서 관용되어 있는 방법에 따라 실시할 수 있다.
(융합 콜라게나제를 발현하는 숙주세포의 배양과 친화성 크로마토그래피에 의한 CBD 를 가진 융합 콜라게나제의 선택적 회수)
본 발명에서는 융합 콜라게나제를 발현하는 숙주세포를 적당한 배지에서 배양하고, 그 배양물로부터 융합 콜라게나제를 얻을 수가 있다. 융합 콜라게나제를 발현하는 숙주세포의 배양 및 그 조건은 사용하는 숙주세포에 대한 그것과 본질적으로 동등하여도 좋다.
융합 콜라게나제를 발현하는 숙주세포 중 또는 배양액 중에 분비된 융합 콜라게나제의 회수는 이 분야에서 관용되어 있는 방법을 이용할 수가 있다.
상기의 방법에 의해 회수된 융합 콜라게나제는 친화성 크로마토그래피에 제공해서 분해 콜라게나제를 제거함으로써, CBD를 가진 융합 콜라게나제를 선택적으로 회수할 수 있게 된다. 이때에 이용되는 친화성 크로마토그래피는 콜라게나제에 결합시킨 친화성 태그에 대응한 방법일 필요가 있는바, 예컨대 히스티딘 태그를 결합시킨 경우에는 히스티딘 태그가 선택적으로 결합되는 니켈 킬레이트 컬럼 등으로 정제하게 된다.
친화성 크로마토그래피에 의한 분해 콜라게나제 제거의 정도는 융합 콜라게나제 용액을 젤라틴이 첨가된 겔에 의해 전기영동하고, 그 후 활성 염색을 함으로써 평가할 수가 있다.
(기타의 태양)
대장균 등으로 조환 콜라게나제를 발현시킨 경우에 그의 CBD의 일부 또는 전부가 분해된다고 하는 본 발명자들의 지견(知見)으로부터, 조환 콜라게나제에서의 CBD에 결합되는 항체를 이용해서 분해된 콜라게나제를 배제하고서 분해되어 있지 않은 조환 콜라게나제를 특이적으로 친화성 정제할 수도 있다. 이 경우, 조환 콜라게나제에 친화성 태그를 융합시킬 필요가 없다는 점에서 유리하다. 즉, 본 발명은 조환 콜라게나제를 발현시킨 숙주세포를 배양하고 얻어지는 배양물을 당해 조환 콜라게나제의 CBD에 결합되는 항체로 정제함으로써, CBD를 가진 콜라게나제를 선택적으로 채취하는 것을 특징으로 하는 콜라게나제의 제조방법도 제공한다. 그리고 CBD와 콜라겐은 친화성를 갖기 때문에, 상기 항체 대신 콜라겐을 이용해서 조환 콜라게나제를 특이적으로 친화성 정제할 수도 있다. 즉, 본 발명은 조환 콜라게나제를 발현시킨 숙주세포를 배양해서 얻어지는 배양물을 콜라겐으로 정제함으로써, CBD를 가진 콜라게나제를 선택적으로 채취하는 것을 특징으로 하는 콜라게나제의 제조방법도 제공한다.
[실시예]
본 발명을 실시예에 의해 보다 구체적으로 설명하는바, 본 발명은 그 요지를 넘지 않는 한 이하의 실시예에 한정되는 것은 아니다.
[실시예 1]클로스트리디움·히스트리티캄 유래의 콜라게나제 G의 카르복실 말단에 히스티딘 태그를 연결한 융합 콜라게나제(융합 콜라게나제 G)의 발현
(1-1) 콜라게나제 G유전자 단편의 조제
클로스트리디움·히스트리티캄 유래의 콜라게나제 G 유전자의 5' 측 말단으로부터 3' 측 말단까지를 클로스트리디움·히스트리티캄 유래의 게놈 DNA를 주형으로 해서 PCR에 의해 증폭시켰다. 이때, 증폭된 콜라게나제 G 유전자의 3' 측 말단이 XbaI 인식 서열로 되고, 또한 본 유전자의 종결 코돈에 이어져 BamHI 인식 서열이 부가되는 프라이머를 설계하였다. 그 결과 비특허문헌 1에 기재된 천연의 콜라게나제 G의 카르복실 말단 아미노산 서열의 2곳에 변이(서열번호:1의 1007번째와 1008번째의 아미노산)가 도입되어, 서열번호:2에 기재된 아미노산 서열로 개변(改變)되었다.
[0057] 본 PCR에 사용된 프라이머는 이하와 같다.
colG-F:
ATGAAAAAAAATATTTTAAAGATTC (서열번호:9)
colG-R:
CCGGATCCTATCTAGATACCCTTAACT (서열번호:10)
증폭된 콜라게나제 G 유전자 단편은 BamHI에 의해 소화되도록 하였다.
(1-2) 히스티딘 태그를 코드하는 영역을 포함된 DNA 단편의 조제
6개의 연속된 히스티딘 잔기로 이루어진 히스티딘 태그를 코드하는 DNA를 제조하기 위해, 시판되고 있는 벡터인 pET-24a(+)를 주형으로 한 PCR을 실시하여, 히스티딘 태그를 코드하는 DNA를 증폭시켰다. 또, 본 DNA 단편에는 히스티딘 태그를 코드하는 DNA에 더해 본 벡터에서 유래하는 다중 클로닝 부위, T7 터미네이터에 대응하는 유전자 단편도 포함되도록 하였다. 본 증폭 DNA 단편의 5' 측 말단에 XbaI 및 3' 측 말단에 BamHI 인식 서열을 포함하는 형태로 프라이머를 설계하였다.
본 PCR에 사용된 프라이머는 이하와 같다.
His-F:
GCTCTAGAAAGCTTGCGGCCGCACTCGA (서열번호:11)
His-R:
CGGGATCCGGATATAGTTCCTCCT (서열번호:12)
증폭된 히스티딘 태그를 코드하는 영역을 포함된 DNA 단편은 XbaI 및 BamHI에 의해 이중소화(二重消化)되도록 하였다.
(1-3) lacZ 프로모터 단편의 제조
융합 콜라게나제를 발현시키기 위한 프로모터로서, lacZ 프로모터를 조제하였다. 본 DNA 단편은 pUC19를 주형으로 한 PCR에 증폭시켰다. 이때, 증폭 DNA 단편의 5'측 말단에 HindIII 인식 서열을 포함하는 형태로 프라이머를 설계하였다.
본 PCR에 사용된 프라이머는 이하와 같다.
lac-F:
CCGGCAAGCTTGCCCAATACGCAAACCG (서열번호:13)
lac-R:
AGCTGTTTCCTGTGTGAA (서열번호:14)
증폭된 lacZ 프로모터 단편은 HindIII에 의해 소화되도록 하였다.
(1-4) 히스티딘 태그를 연결한 융합 콜라게나제 G의 발현 벡터의 구축
상기의 방법으로 조제한 3종의 DNA 단편을 5' 측 말단으로부터 lacZ 프로모터, 콜라게나제 G 유전자, 히스티딘 태그를 포함한 DNA 단편의 순으로 연결되도록, 시판되고 있는 벡터인 pBR322에 삽입하였다. 먼저, lacZ 프로모터, 콜라게나제 G 유전자를 pBR322에 삽입하였다. 즉, 상기와 같이 조제한 lacZ 프로모터 영역, 및 콜라게나제 G 유전자 단편을 인산화한 후, HindIII 및 BamHI로 이중소화시킨 pBR322에 삽입하여 pColG(도 1)를 구축하였다. 한편, lacZ 유전자 프로모터 영역(PlacZ)과 colG 유전자의 연결은 평활 말단에서 실행하였다. 계속해서, XbaI 및 BamHI에서 이중소화시킨 pColG에, 상기의 방법으로 조제한 히스티딘 태그를 코드하는 DNA를 삽입하여 pColG-His(도 2)를 구축하였다. 최종적으로 pBR322에 삽입된 DNA는 서열표:4에 기재된 1번에서 3396번까지의 염기서열을 가진 DNA로 되었다.
(1-5) 융합 콜라게나제 G 발현 대장균의 도출
통상적인 방법에 따라 pColG-His를 대장균 Escherichia coli χ1776 균주에 형질전환하고, 20μg/ml의 디아미노피메린산, 100μg/ml 티미딘, 50μg/ml 암피실린을 첨가한 LB 한천 배지에서 37℃, 하루 밤낮 배양하여, 융합 콜라게나제 G 발현 대장균을 도출하였다.
[실시예 2]융합 콜라게나제 G 발현 대장균의 배양, 및 CBD를 가진 콜라게나제 G의 선택적 회수
(2-1) 융합 콜라게나제 G 발현 대장균의 배양
실시예 1에서 얻은 융합 콜라게나제 G 발현 대장균을 100ml의 배지를 가한 250ml의 삼각 플라스크에 식균(植菌)하고서, 200rpm에서 28℃, 16시간 교반해서 배양하였다. 본 배양에 사용한 배지는 100μg/ml의 디아미노피메린산, 20μg/ml 티미딘, 50μg/ml 암피실린, 0.1 mM의 IPTG를 첨가한 TB 배지(1.2% 트립톤, 2.4% 이스트 추출물, 0.94% 인산 수소 2칼륨, 0.22% 인산 2수소 칼륨, 0.8% 글리세롤)로 하였다.
(2-2) 융합 콜라게나제 G 발현 대장균의 추출액 제조
(2-1)에서 얻어진 배양 종료액을 원심분리함으로써 균체를 회수하고, 회수된 균체를 10ml의 POP culture Regent(머크사 제)에서 용균시켜, 균체 내의 단백질을 추출하였다. 용균액의 원심분리에 의해 얻어지는 상청(上淸)을, 유전자 조환체를 제거하기 위해 0.2μm의 막으로 여과하여, 융합 콜라게나제 G 발현 대장균의 추출액으로 하였다.
(2-3) 친화성 크로마토그래피에 의한 CBD를 가진 융합 콜라게나제 G의 선택적 회수
(2-2)에서 얻어진 융합 콜라게나제 G 발현 대장균의 추출액으로부터 분해 콜라게나제를 제거하기 위해, 히스티딘 태그에 대한 친화성 크로마토그래피인 니켈 킬레이트 컬럼에 의한 분획을 실행하였다. 상기의 방법으로 제조한 융합 콜라게나제 G 발현 대장균의 추출액 10ml에, 60ml의 니켈 킬레이트 컬럼 결합용 완충액(0.5M의 NaCl, 20 mM 이미다졸을 첨가한 20mM의 인산나트륨 완충액(pH7.5))을 첨가하고, 니켈 킬레이트 컬럼 결합용 완충액으로 평형화한 100ml의 니켈 킬레이트 컬럼에 통과(通液)시켯였다. 그 후, 적당량의 니켈 킬레이트 컬럼 결합용 완충액으로 컬럼 세정하고, 니켈 킬레이트 컬럼에 흡착될 수 없는 분해 콜라게나제를 제거한 후에, 500mM의 이미다졸을 첨가한 니켈 킬레이트 컬럼 결합용 완충액 100ml를 통과시켜, CBD를 가진 융합 콜라게나제 G를 회수하였다.
(2-4) 분해 콜라게나제 제거의 확인
융합 콜라게나제 G 추출액으로부터의 분해 콜라게나제의 제거를 확인하기 위해, 융합 콜라게나제 G 발현 대장균의 추출액 및 친화성 크로마토그래피에 제공한 융합 콜라게나제 G 용액에 대해 활성 염색을 실시하였다. (2-2)에서 얻어진 융합 콜라게나제 G 발현 대장균의 추출액 0.25μl 및 (2-3)에서 얻어진 친화성 크로마토그래피에 제공한 융합 콜라게나제 G 용액 2.5μl를 Zymogram-PAGE mini(테프코사 제)에 제공하여 활성 염색을 실시하였다. 그 결과, 융합 콜라게나제 G 발현 대장균의 추출액에는 프로테아제 활성을 나타내는 5개의 밴드가 관찰되었다(도 3). 한편, 친화성 크로마토그래피에 제공한 융합 콜라게나제 G 용액은, 상기의 5개의 밴드 중, 최대의 분자량을 나타내는 1개의 밴드가 주요한 밴드로서 관찰되었다(도 4). 이들 밴드의 비교와 분석으로부터 대장균으로 융합 콜라게나제 G를 발현시켰을 경우, CBD의 일부 또는 전부가 분해되는 것이 판명되었다. 이상의 결과로부터 융합 콜라게나제 G 발현 대장균의 추출액을 친화성 크로마토그래피에 의해 정제함으로써, CBD의 일부 또는 전부가 분해된 콜라게나제를 제거하여, CBD를 가진 융합 콜라게나제를 선택적으로 회수할 수 있다는 것을 알게 되었다.
[실시예 3]클로스트리디움·히스트리티캄 유래의 콜라게나제 H의 카르복실 말단에 히스티딘 태그를 연결한 융합 콜라게나제의 발현
(3-1) 콜라게나제 H 유전자 단편의 제조
클로스트리디움·히스트리티캄 유래의 콜라게나제 H 유전자의 5' 측 말단에서부터 3'측 말단까지를 클로스트리디움·히스트리티캄 유래의 게놈 DNA를 주형으로 한 PCR에 의해 증폭시켰다. 이때 증폭된 콜라게나제 H 유전자의 3' 측 말단 이 XbaI 인식 서열로 되고, 또 본 유전자의 종결 코돈에 이어져 BamHI 인식 서열이 부가되는 프라이머를 설계하였다. 그 결과, 비특허문헌 2에 기재된 천연의 콜라게나제 H의 아미노산 서열의 카르복실 말단 아미노산 서열 1곳에 변이(서열번호:5의 980번째의 아미노산)가 도입되어, 서열번호:6에 기재된 아미노산 서열로 개변되었다.
본 PCR에 사용된 프라이머는 이하와 같다.
colH-F:
ATGAAAAGGAAATGTTTATC (서열번호:15)
colH-R:
CCGGATCCTATCTAGATACTGAACCTT (서열번호:16)
증폭된 콜라게나제 H 유전자 단편은 BamHI에 의해 소화되었다.
(3-2) 히스티딘 태그를 코드하는 영역을 포함한 DNA 단편의 제조
히스티딘 태그를 코드하는 영역을 포함한 DNA 단편은 실시예 1과 마찬가지 방법으로 제조하였다.
(3-3) lacZ 프로모터 단편의 제조
lacZ 프로모터 단편은 실시예 1과 마찬가지 방법으로 제조하였다.
(3-4) 히스티딘 태그를 연결한 융합 콜라게나제 H의 발현 벡터의 구축
상기의 방법으로 제조한 3종의 DNA 단편을, 5' 측 말단에서부터 lacZ 프로모터, 콜라게나제 H 유전자, 히스티딘 태그를 포함된 DNA 단편의 순으로 연결되도록, 시판되고 있는 벡터인 pBR322에 삽입하였다. 먼저, lacZ 프로모터, 콜라게나제 H 유전자를 pBR322에 삽입하기 위해, 상기와 같이 제조한 lacZ 프로모터 영역, 및 콜라게나제 H유전자 단편을 인산화한 후, HindIII 및 BamHI으로 이중소화시킨 pBR322에 삽입하여 pColH(도 5)를 구축하였다. 한편, lacZ 유전자 프로모터 영역과 콜라게나제 H 유전자의 연결은 평활 말단에서 실행하였다. 계속해서, XbaI 및 BamHI으로 이중소화시킨 pColH에, 상기의 방법으로 제조한 히스티딘 태그를 코드하는 DNA를 포함한 DNA 단편을 삽입하여 pColH-His(도 6)를 구축하였다. 최종적으로 pBR322에 삽입된 DNA는 서열표:8에 기재된 1번에서 3105번까지의 염기서열을 가진 DNA로 되었다.
(3-5) 융합 콜라게나제 H 발현 대장균의 도출
융합 콜라게나제 H 발현 대장균은 실시예 1과 마찬가지 방법으로 도출되었다.
[실시예 4]융합 콜라게나제 H 발현 대장균의 배양, 및 CBD를 가진 융합 콜라게나제 H의 선택적 회수
(4-1) 융합 콜라게나제 H 발현 대장균의 배양
실시예 3에서 얻은 융합 콜라게나제 H 발현 대장균을 실시예 2에 기재된 방법으로 배양하여 배양액을 얻었다.
(4-2) 융합 콜라게나제 H 발현 대장균의 추출액의 제조
(4-1)에서 얻어진 배양 종료액으로부터 실시예 2에 기재된 방법으로 융합 콜라게나제 H 발현 대장균의 추출액을 얻었다.
(4-3) 친화성 크로마토그래피에 의한 CBD를 가진 융합 콜라게나제 H의 선택적 회수
(4-2)에서 얻어진 융합 콜라게나제 H 발현 대장균의 추출액을 실시예 2에 기재된 방법으로 친화성 크로마토그래피에 제공하여 CBD를 가진 융합 콜라게나제 H를 회수하였다.
(4-4) 분해 콜라게나제 제거의 확인
융합 콜라게나제 H로부터의 분해 콜라게나제의 제거의 정도를 확인하기 위해, 실시예 2에 기재된 방법으로 전기영동 후에 활성 염색을 실시하였다. 그 결과, 융합 콜라게나제 H 발현 대장균의 추출액에는 프로테아제 활성을 나타내는 4개의 밴드가 관찰되었다(도 7). 한편, 친화성 크로마토그래피에 제공한 융합 콜라게나제 H 용액은 상기 4개의 밴드 중 최대의 분자량을 나타내는 1개의 밴드가 주요한 밴드로서 관찰되었다(도 8). 이들 밴드의 비교와 분석으로부터 대장균으로 발현시킨 융합 콜라게나제 H에서의 CBD의 일부 또는 전부가 분해된 것이 판명되었다. 이상의 결과로부터 융합 콜라게나제 H 발현 대장균의 추출액을 친화성 크로마토그래피로 정제함으로써, CBD의 일부 또는 전부가 분해된 콜라게나제를 제거하여 CBD를 가진 융합 콜라게나제 H를 선택적으로 회수할 수 있게 되었다.
본 발명에 의하면, 조환 단백질로서의 콜라게나제를 숙주의 작용에 의한 분해 산물을 함유하지 않도록, 높은 순도로 생산할 수가 있다. 본 발명의 방법으로 생산된 콜라게나제를 쓰게 되면, 예컨대 췌도의 질을 저하시키지 않고 췌장으로부터의 췌도를 분리할 수가 있기 때문에, 당뇨병 환자에의 췌도 이식에 크게 공헌할 수 있는 것이다.
SEQUENCE LISTING
<110> MEIJI SEIKA KAISHA, LTD.
TOHOKU UNIVERSITY
<120> A Collagenase with an affinity tag, and its preparation method
<130> M0833
<150> JP 2008-295922
<151> 2008-11-19
<160> 16
<170> PatentIn version 3.1
<210> 1
<211> 1118
<212> PRT
<213> Clostridium histolyticum
<220>
<221> SIGNAL
<222> (-110)..(-1)
<220>
<221> mat_peptide
<222> (1)..(1008)
<400> 1
Met Lys Lys Asn Ile Leu Lys Ile Leu Met Asp Ser Tyr Ser Lys
-110 -105 -100
Glu Ser Lys Ile Gln Thr Val Arg Arg Val Thr Ser Val Ser Leu Leu
-95 -90 -85 -80
Ala Val Tyr Leu Thr Met Asn Thr Ser Ser Leu Val Leu Ala Lys Pro
-75 -70 -65
Ile Glu Asn Thr Asn Asp Thr Ser Ile Lys Asn Val Glu Lys Leu Arg
-60 -55 -50
Asn Ala Pro Asn Glu Glu Asn Ser Lys Lys Val Glu Asp Ser Lys Asn
-45 -40 -35
Asp Lys Val Glu His Val Lys Asn Ile Glu Glu Ala Lys Val Glu Gln
-30 -25 -20
Val Ala Pro Glu Val Lys Ser Lys Ser Thr Leu Arg Ser Ala Ser Ile
-15 -10 -5 -1 1
Ala Asn Thr Asn Ser Glu Lys Tyr Asp Phe Glu Tyr Leu Asn Gly Leu
5 10 15
Ser Tyr Thr Glu Leu Thr Asn Leu Ile Lys Asn Ile Lys Trp Asn Gln
20 25 30
Ile Asn Gly Leu Phe Asn Tyr Ser Thr Gly Ser Gln Lys Phe Phe Gly
35 40 45
Asp Lys Asn Arg Val Gln Ala Ile Ile Asn Ala Leu Gln Glu Ser Gly
50 55 60 65
Arg Thr Tyr Thr Ala Asn Asp Met Lys Gly Ile Glu Thr Phe Thr Glu
70 75 80
Val Leu Arg Ala Gly Phe Tyr Leu Gly Tyr Tyr Asn Asp Gly Leu Ser
85 90 95
Tyr Leu Asn Asp Arg Asn Phe Gln Asp Lys Cys Ile Pro Ala Met Ile
100 105 110
Ala Ile Gln Lys Asn Pro Asn Phe Lys Leu Gly Thr Ala Val Gln Asp
115 120 125
Glu Val Ile Thr Ser Leu Gly Lys Leu Ile Gly Asn Ala Ser Ala Asn
130 135 140 145
Ala Glu Val Val Asn Asn Cys Val Pro Val Leu Lys Gln Phe Arg Glu
150 155 160
Asn Leu Asn Gln Tyr Ala Pro Asp Tyr Val Lys Gly Thr Ala Val Asn
165 170 175
Glu Leu Ile Lys Gly Ile Glu Phe Asp Phe Ser Gly Ala Ala Tyr Glu
180 185 190
Lys Asp Val Lys Thr Met Pro Trp Tyr Gly Lys Ile Asp Pro Phe Ile
195 200 205
Asn Glu Leu Lys Ala Leu Gly Leu Tyr Gly Asn Ile Thr Ser Ala Thr
210 215 220 225
Glu Trp Ala Ser Asp Val Gly Ile Tyr Tyr Leu Ser Lys Phe Gly Leu
230 235 240
Tyr Ser Thr Asn Arg Asn Asp Ile Val Gln Ser Leu Glu Lys Ala Val
245 250 255
Asp Met Tyr Lys Tyr Gly Lys Ile Ala Phe Val Ala Met Glu Arg Ile
260 265 270
Thr Trp Asp Tyr Asp Gly Ile Gly Ser Asn Gly Lys Lys Val Asp His
275 280 285
Asp Lys Phe Leu Asp Asp Ala Glu Lys His Tyr Leu Pro Lys Thr Tyr
290 295 300 305
Thr Phe Asp Asn Gly Thr Phe Ile Ile Arg Ala Gly Asp Lys Val Ser
310 315 320
Glu Glu Lys Ile Lys Arg Leu Tyr Trp Ala Ser Arg Glu Val Lys Ser
325 330 335
Gln Phe His Arg Val Val Gly Asn Asp Lys Ala Leu Glu Val Gly Asn
340 345 350
Ala Asp Asp Val Leu Thr Met Lys Ile Phe Asn Ser Pro Glu Glu Tyr
355 360 365
Lys Phe Asn Thr Asn Ile Asn Gly Val Ser Thr Asp Asn Gly Gly Leu
370 375 380 385
Tyr Ile Glu Pro Arg Gly Thr Phe Tyr Thr Tyr Glu Arg Thr Pro Gln
390 395 400
Gln Ser Ile Phe Ser Leu Glu Glu Leu Phe Arg His Glu Tyr Thr His
405 410 415
Tyr Leu Gln Ala Arg Tyr Leu Val Asp Gly Leu Trp Gly Gln Gly Pro
420 425 430
Phe Tyr Glu Lys Asn Arg Leu Thr Trp Phe Asp Glu Gly Thr Ala Glu
435 440 445
Phe Phe Ala Gly Ser Thr Arg Thr Ser Gly Val Leu Pro Arg Lys Ser
450 455 460 465
Ile Leu Gly Tyr Leu Ala Lys Asp Lys Val Asp His Arg Tyr Ser Leu
470 475 480
Lys Lys Thr Leu Asn Ser Gly Tyr Asp Asp Ser Asp Trp Met Phe Tyr
485 490 495
Asn Tyr Gly Phe Ala Val Ala His Tyr Leu Tyr Glu Lys Asp Met Pro
500 505 510
Thr Phe Ile Lys Met Asn Lys Ala Ile Leu Asn Thr Asp Val Lys Ser
515 520 525
Tyr Asp Glu Ile Ile Lys Lys Leu Ser Asp Asp Ala Asn Lys Asn Thr
530 535 540 545
Glu Tyr Gln Asn His Ile Gln Glu Leu Ala Asp Lys Tyr Gln Gly Ala
550 555 560
Gly Ile Pro Leu Val Ser Asp Asp Tyr Leu Lys Asp His Gly Tyr Lys
565 570 575
Lys Ala Ser Glu Val Tyr Ser Glu Ile Ser Lys Ala Ala Ser Leu Thr
580 585 590
Asn Thr Ser Val Thr Ala Glu Lys Ser Gln Tyr Phe Asn Thr Phe Thr
595 600 605
Leu Arg Gly Thr Tyr Thr Gly Glu Thr Ser Lys Gly Glu Phe Lys Asp
610 615 620 625
Trp Asp Glu Met Ser Lys Lys Leu Asp Gly Thr Leu Glu Ser Leu Ala
630 635 640
Lys Asn Ser Trp Ser Gly Tyr Lys Thr Leu Thr Ala Tyr Phe Thr Asn
645 650 655
Tyr Arg Val Thr Ser Asp Asn Lys Val Gln Tyr Asp Val Val Phe His
660 665 670
Gly Val Leu Thr Asp Asn Ala Asp Ile Ser Asn Asn Lys Ala Pro Ile
675 680 685
Ala Lys Val Thr Gly Pro Ser Thr Gly Ala Val Gly Arg Asn Ile Glu
690 695 700 705
Phe Ser Gly Lys Asp Ser Lys Asp Glu Asp Gly Lys Ile Val Ser Tyr
710 715 720
Asp Trp Asp Phe Gly Asp Gly Ala Thr Ser Arg Gly Lys Asn Ser Val
725 730 735
His Ala Tyr Lys Lys Ala Gly Thr Tyr Asn Val Thr Leu Lys Val Thr
740 745 750
Asp Asp Lys Gly Ala Thr Ala Thr Glu Ser Phe Thr Ile Glu Ile Lys
755 760 765
Asn Glu Asp Thr Thr Thr Pro Ile Thr Lys Glu Met Glu Pro Asn Asp
770 775 780 785
Asp Ile Lys Glu Ala Asn Gly Pro Ile Val Glu Gly Val Thr Val Lys
790 795 800
Gly Asp Leu Asn Gly Ser Asp Asp Ala Asp Thr Phe Tyr Phe Asp Val
805 810 815
Lys Glu Asp Gly Asp Val Thr Ile Glu Leu Pro Tyr Ser Gly Ser Ser
820 825 830
Asn Phe Thr Trp Leu Val Tyr Lys Glu Gly Asp Asp Gln Asn His Ile
835 840 845
Ala Ser Gly Ile Asp Lys Asn Asn Ser Lys Val Gly Thr Phe Lys Ser
850 855 860 865
Thr Lys Gly Arg His Tyr Val Phe Ile Tyr Lys His Asp Ser Ala Ser
870 875 880
Asn Ile Ser Tyr Ser Leu Asn Ile Lys Gly Leu Gly Asn Glu Lys Leu
885 890 895
Lys Glu Lys Glu Asn Asn Asp Ser Ser Asp Lys Ala Thr Val Ile Pro
900 905 910
Asn Phe Asn Thr Thr Met Gln Gly Ser Leu Leu Gly Asp Asp Ser Arg
915 920 925
Asp Tyr Tyr Ser Phe Glu Val Lys Glu Glu Gly Glu Val Asn Ile Glu
930 935 940 945
Leu Asp Lys Lys Asp Glu Phe Gly Val Thr Trp Thr Leu His Pro Glu
950 955 960
Ser Asn Ile Asn Asp Arg Ile Thr Tyr Gly Gln Val Asp Gly Asn Lys
965 970 975
Val Ser Asn Lys Val Lys Leu Arg Pro Gly Lys Tyr Tyr Leu Leu Val
980 985 990
Tyr Lys Tyr Ser Gly Ser Gly Asn Tyr Glu Leu Arg Val Asn Lys
995 1000 1005
<210> 2
<211> 1118
<212> PRT
<213> Clostridium histolyticum
<220>
<221> SIGNAL
<222> (-110)..(-1)
<220>
<221> mat_peptide
<222> (1)..(1008)
<400> 2
Met Lys Lys Asn Ile Leu Lys Ile Leu Met Asp Ser Tyr Ser Lys
-110 -105 -100
Glu Ser Lys Ile Gln Thr Val Arg Arg Val Thr Ser Val Ser Leu Leu
-95 -90 -85 -80
Ala Val Tyr Leu Thr Met Asn Thr Ser Ser Leu Val Leu Ala Lys Pro
-75 -70 -65
Ile Glu Asn Thr Asn Asp Thr Ser Ile Lys Asn Val Glu Lys Leu Arg
-60 -55 -50
Asn Ala Pro Asn Glu Glu Asn Ser Lys Lys Val Glu Asp Ser Lys Asn
-45 -40 -35
Asp Lys Val Glu His Val Lys Asn Ile Glu Glu Ala Lys Val Glu Gln
-30 -25 -20
Val Ala Pro Glu Val Lys Ser Lys Ser Thr Leu Arg Ser Ala Ser Ile
-15 -10 -5 -1 1
Ala Asn Thr Asn Ser Glu Lys Tyr Asp Phe Glu Tyr Leu Asn Gly Leu
5 10 15
Ser Tyr Thr Glu Leu Thr Asn Leu Ile Lys Asn Ile Lys Trp Asn Gln
20 25 30
Ile Asn Gly Leu Phe Asn Tyr Ser Thr Gly Ser Gln Lys Phe Phe Gly
35 40 45
Asp Lys Asn Arg Val Gln Ala Ile Ile Asn Ala Leu Gln Glu Ser Gly
50 55 60 65
Arg Thr Tyr Thr Ala Asn Asp Met Lys Gly Ile Glu Thr Phe Thr Glu
70 75 80
Val Leu Arg Ala Gly Phe Tyr Leu Gly Tyr Tyr Asn Asp Gly Leu Ser
85 90 95
Tyr Leu Asn Asp Arg Asn Phe Gln Asp Lys Cys Ile Pro Ala Met Ile
100 105 110
Ala Ile Gln Lys Asn Pro Asn Phe Lys Leu Gly Thr Ala Val Gln Asp
115 120 125
Glu Val Ile Thr Ser Leu Gly Lys Leu Ile Gly Asn Ala Ser Ala Asn
130 135 140 145
Ala Glu Val Val Asn Asn Cys Val Pro Val Leu Lys Gln Phe Arg Glu
150 155 160
Asn Leu Asn Gln Tyr Ala Pro Asp Tyr Val Lys Gly Thr Ala Val Asn
165 170 175
Glu Leu Ile Lys Gly Ile Glu Phe Asp Phe Ser Gly Ala Ala Tyr Glu
180 185 190
Lys Asp Val Lys Thr Met Pro Trp Tyr Gly Lys Ile Asp Pro Phe Ile
195 200 205
Asn Glu Leu Lys Ala Leu Gly Leu Tyr Gly Asn Ile Thr Ser Ala Thr
210 215 220 225
Glu Trp Ala Ser Asp Val Gly Ile Tyr Tyr Leu Ser Lys Phe Gly Leu
230 235 240
Tyr Ser Thr Asn Arg Asn Asp Ile Val Gln Ser Leu Glu Lys Ala Val
245 250 255
Asp Met Tyr Lys Tyr Gly Lys Ile Ala Phe Val Ala Met Glu Arg Ile
260 265 270
Thr Trp Asp Tyr Asp Gly Ile Gly Ser Asn Gly Lys Lys Val Asp His
275 280 285
Asp Lys Phe Leu Asp Asp Ala Glu Lys His Tyr Leu Pro Lys Thr Tyr
290 295 300 305
Thr Phe Asp Asn Gly Thr Phe Ile Ile Arg Ala Gly Asp Lys Val Ser
310 315 320
Glu Glu Lys Ile Lys Arg Leu Tyr Trp Ala Ser Arg Glu Val Lys Ser
325 330 335
Gln Phe His Arg Val Val Gly Asn Asp Lys Ala Leu Glu Val Gly Asn
340 345 350
Ala Asp Asp Val Leu Thr Met Lys Ile Phe Asn Ser Pro Glu Glu Tyr
355 360 365
Lys Phe Asn Thr Asn Ile Asn Gly Val Ser Thr Asp Asn Gly Gly Leu
370 375 380 385
Tyr Ile Glu Pro Arg Gly Thr Phe Tyr Thr Tyr Glu Arg Thr Pro Gln
390 395 400
Gln Ser Ile Phe Ser Leu Glu Glu Leu Phe Arg His Glu Tyr Thr His
405 410 415
Tyr Leu Gln Ala Arg Tyr Leu Val Asp Gly Leu Trp Gly Gln Gly Pro
420 425 430
Phe Tyr Glu Lys Asn Arg Leu Thr Trp Phe Asp Glu Gly Thr Ala Glu
435 440 445
Phe Phe Ala Gly Ser Thr Arg Thr Ser Gly Val Leu Pro Arg Lys Ser
450 455 460 465
Ile Leu Gly Tyr Leu Ala Lys Asp Lys Val Asp His Arg Tyr Ser Leu
470 475 480
Lys Lys Thr Leu Asn Ser Gly Tyr Asp Asp Ser Asp Trp Met Phe Tyr
485 490 495
Asn Tyr Gly Phe Ala Val Ala His Tyr Leu Tyr Glu Lys Asp Met Pro
500 505 510
Thr Phe Ile Lys Met Asn Lys Ala Ile Leu Asn Thr Asp Val Lys Ser
515 520 525
Tyr Asp Glu Ile Ile Lys Lys Leu Ser Asp Asp Ala Asn Lys Asn Thr
530 535 540 545
Glu Tyr Gln Asn His Ile Gln Glu Leu Ala Asp Lys Tyr Gln Gly Ala
550 555 560
Gly Ile Pro Leu Val Ser Asp Asp Tyr Leu Lys Asp His Gly Tyr Lys
565 570 575
Lys Ala Ser Glu Val Tyr Ser Glu Ile Ser Lys Ala Ala Ser Leu Thr
580 585 590
Asn Thr Ser Val Thr Ala Glu Lys Ser Gln Tyr Phe Asn Thr Phe Thr
595 600 605
Leu Arg Gly Thr Tyr Thr Gly Glu Thr Ser Lys Gly Glu Phe Lys Asp
610 615 620 625
Trp Asp Glu Met Ser Lys Lys Leu Asp Gly Thr Leu Glu Ser Leu Ala
630 635 640
Lys Asn Ser Trp Ser Gly Tyr Lys Thr Leu Thr Ala Tyr Phe Thr Asn
645 650 655
Tyr Arg Val Thr Ser Asp Asn Lys Val Gln Tyr Asp Val Val Phe His
660 665 670
Gly Val Leu Thr Asp Asn Ala Asp Ile Ser Asn Asn Lys Ala Pro Ile
675 680 685
Ala Lys Val Thr Gly Pro Ser Thr Gly Ala Val Gly Arg Asn Ile Glu
690 695 700 705
Phe Ser Gly Lys Asp Ser Lys Asp Glu Asp Gly Lys Ile Val Ser Tyr
710 715 720
Asp Trp Asp Phe Gly Asp Gly Ala Thr Ser Arg Gly Lys Asn Ser Val
725 730 735
His Ala Tyr Lys Lys Ala Gly Thr Tyr Asn Val Thr Leu Lys Val Thr
740 745 750
Asp Asp Lys Gly Ala Thr Ala Thr Glu Ser Phe Thr Ile Glu Ile Lys
755 760 765
Asn Glu Asp Thr Thr Thr Pro Ile Thr Lys Glu Met Glu Pro Asn Asp
770 775 780 785
Asp Ile Lys Glu Ala Asn Gly Pro Ile Val Glu Gly Val Thr Val Lys
790 795 800
Gly Asp Leu Asn Gly Ser Asp Asp Ala Asp Thr Phe Tyr Phe Asp Val
805 810 815
Lys Glu Asp Gly Asp Val Thr Ile Glu Leu Pro Tyr Ser Gly Ser Ser
820 825 830
Asn Phe Thr Trp Leu Val Tyr Lys Glu Gly Asp Asp Gln Asn His Ile
835 840 845
Ala Ser Gly Ile Asp Lys Asn Asn Ser Lys Val Gly Thr Phe Lys Ser
850 855 860 865
Thr Lys Gly Arg His Tyr Val Phe Ile Tyr Lys His Asp Ser Ala Ser
870 875 880
Asn Ile Ser Tyr Ser Leu Asn Ile Lys Gly Leu Gly Asn Glu Lys Leu
885 890 895
Lys Glu Lys Glu Asn Asn Asp Ser Ser Asp Lys Ala Thr Val Ile Pro
900 905 910
Asn Phe Asn Thr Thr Met Gln Gly Ser Leu Leu Gly Asp Asp Ser Arg
915 920 925
Asp Tyr Tyr Ser Phe Glu Val Lys Glu Glu Gly Glu Val Asn Ile Glu
930 935 940 945
Leu Asp Lys Lys Asp Glu Phe Gly Val Thr Trp Thr Leu His Pro Glu
950 955 960
Ser Asn Ile Asn Asp Arg Ile Thr Tyr Gly Gln Val Asp Gly Asn Lys
965 970 975
Val Ser Asn Lys Val Lys Leu Arg Pro Gly Lys Tyr Tyr Leu Leu Val
980 985 990
Tyr Lys Tyr Ser Gly Ser Gly Asn Tyr Glu Leu Arg Val Ser Arg
995 1000 1005
<210> 3
<211> 1131
<212> PRT
<213> Clostridium histolyticum
<220>
<221> SIGNAL
<222> (-110)..(-1)
<220>
<221> mat_peptide
<222> (1)..(1021)
<400> 3
Met Lys Lys Asn Ile Leu Lys Ile Leu Met Asp Ser Tyr Ser Lys
-110 -105 -100
Glu Ser Lys Ile Gln Thr Val Arg Arg Val Thr Ser Val Ser Leu Leu
-95 -90 -85 -80
Ala Val Tyr Leu Thr Met Asn Thr Ser Ser Leu Val Leu Ala Lys Pro
-75 -70 -65
Ile Glu Asn Thr Asn Asp Thr Ser Ile Lys Asn Val Glu Lys Leu Arg
-60 -55 -50
Asn Ala Pro Asn Glu Glu Asn Ser Lys Lys Val Glu Asp Ser Lys Asn
-45 -40 -35
Asp Lys Val Glu His Val Lys Asn Ile Glu Glu Ala Lys Val Glu Gln
-30 -25 -20
Val Ala Pro Glu Val Lys Ser Lys Ser Thr Leu Arg Ser Ala Ser Ile
-15 -10 -5 -1 1
Ala Asn Thr Asn Ser Glu Lys Tyr Asp Phe Glu Tyr Leu Asn Gly Leu
5 10 15
Ser Tyr Thr Glu Leu Thr Asn Leu Ile Lys Asn Ile Lys Trp Asn Gln
20 25 30
Ile Asn Gly Leu Phe Asn Tyr Ser Thr Gly Ser Gln Lys Phe Phe Gly
35 40 45
Asp Lys Asn Arg Val Gln Ala Ile Ile Asn Ala Leu Gln Glu Ser Gly
50 55 60 65
Arg Thr Tyr Thr Ala Asn Asp Met Lys Gly Ile Glu Thr Phe Thr Glu
70 75 80
Val Leu Arg Ala Gly Phe Tyr Leu Gly Tyr Tyr Asn Asp Gly Leu Ser
85 90 95
Tyr Leu Asn Asp Arg Asn Phe Gln Asp Lys Cys Ile Pro Ala Met Ile
100 105 110
Ala Ile Gln Lys Asn Pro Asn Phe Lys Leu Gly Thr Ala Val Gln Asp
115 120 125
Glu Val Ile Thr Ser Leu Gly Lys Leu Ile Gly Asn Ala Ser Ala Asn
130 135 140 145
Ala Glu Val Val Asn Asn Cys Val Pro Val Leu Lys Gln Phe Arg Glu
150 155 160
Asn Leu Asn Gln Tyr Ala Pro Asp Tyr Val Lys Gly Thr Ala Val Asn
165 170 175
Glu Leu Ile Lys Gly Ile Glu Phe Asp Phe Ser Gly Ala Ala Tyr Glu
180 185 190
Lys Asp Val Lys Thr Met Pro Trp Tyr Gly Lys Ile Asp Pro Phe Ile
195 200 205
Asn Glu Leu Lys Ala Leu Gly Leu Tyr Gly Asn Ile Thr Ser Ala Thr
210 215 220 225
Glu Trp Ala Ser Asp Val Gly Ile Tyr Tyr Leu Ser Lys Phe Gly Leu
230 235 240
Tyr Ser Thr Asn Arg Asn Asp Ile Val Gln Ser Leu Glu Lys Ala Val
245 250 255
Asp Met Tyr Lys Tyr Gly Lys Ile Ala Phe Val Ala Met Glu Arg Ile
260 265 270
Thr Trp Asp Tyr Asp Gly Ile Gly Ser Asn Gly Lys Lys Val Asp His
275 280 285
Asp Lys Phe Leu Asp Asp Ala Glu Lys His Tyr Leu Pro Lys Thr Tyr
290 295 300 305
Thr Phe Asp Asn Gly Thr Phe Ile Ile Arg Ala Gly Asp Lys Val Ser
310 315 320
Glu Glu Lys Ile Lys Arg Leu Tyr Trp Ala Ser Arg Glu Val Lys Ser
325 330 335
Gln Phe His Arg Val Val Gly Asn Asp Lys Ala Leu Glu Val Gly Asn
340 345 350
Ala Asp Asp Val Leu Thr Met Lys Ile Phe Asn Ser Pro Glu Glu Tyr
355 360 365
Lys Phe Asn Thr Asn Ile Asn Gly Val Ser Thr Asp Asn Gly Gly Leu
370 375 380 385
Tyr Ile Glu Pro Arg Gly Thr Phe Tyr Thr Tyr Glu Arg Thr Pro Gln
390 395 400
Gln Ser Ile Phe Ser Leu Glu Glu Leu Phe Arg His Glu Tyr Thr His
405 410 415
Tyr Leu Gln Ala Arg Tyr Leu Val Asp Gly Leu Trp Gly Gln Gly Pro
420 425 430
Phe Tyr Glu Lys Asn Arg Leu Thr Trp Phe Asp Glu Gly Thr Ala Glu
435 440 445
Phe Phe Ala Gly Ser Thr Arg Thr Ser Gly Val Leu Pro Arg Lys Ser
450 455 460 465
Ile Leu Gly Tyr Leu Ala Lys Asp Lys Val Asp His Arg Tyr Ser Leu
470 475 480
Lys Lys Thr Leu Asn Ser Gly Tyr Asp Asp Ser Asp Trp Met Phe Tyr
485 490 495
Asn Tyr Gly Phe Ala Val Ala His Tyr Leu Tyr Glu Lys Asp Met Pro
500 505 510
Thr Phe Ile Lys Met Asn Lys Ala Ile Leu Asn Thr Asp Val Lys Ser
515 520 525
Tyr Asp Glu Ile Ile Lys Lys Leu Ser Asp Asp Ala Asn Lys Asn Thr
530 535 540 545
Glu Tyr Gln Asn His Ile Gln Glu Leu Ala Asp Lys Tyr Gln Gly Ala
550 555 560
Gly Ile Pro Leu Val Ser Asp Asp Tyr Leu Lys Asp His Gly Tyr Lys
565 570 575
Lys Ala Ser Glu Val Tyr Ser Glu Ile Ser Lys Ala Ala Ser Leu Thr
580 585 590
Asn Thr Ser Val Thr Ala Glu Lys Ser Gln Tyr Phe Asn Thr Phe Thr
595 600 605
Leu Arg Gly Thr Tyr Thr Gly Glu Thr Ser Lys Gly Glu Phe Lys Asp
610 615 620 625
Trp Asp Glu Met Ser Lys Lys Leu Asp Gly Thr Leu Glu Ser Leu Ala
630 635 640
Lys Asn Ser Trp Ser Gly Tyr Lys Thr Leu Thr Ala Tyr Phe Thr Asn
645 650 655
Tyr Arg Val Thr Ser Asp Asn Lys Val Gln Tyr Asp Val Val Phe His
660 665 670
Gly Val Leu Thr Asp Asn Ala Asp Ile Ser Asn Asn Lys Ala Pro Ile
675 680 685
Ala Lys Val Thr Gly Pro Ser Thr Gly Ala Val Gly Arg Asn Ile Glu
690 695 700 705
Phe Ser Gly Lys Asp Ser Lys Asp Glu Asp Gly Lys Ile Val Ser Tyr
710 715 720
Asp Trp Asp Phe Gly Asp Gly Ala Thr Ser Arg Gly Lys Asn Ser Val
725 730 735
His Ala Tyr Lys Lys Ala Gly Thr Tyr Asn Val Thr Leu Lys Val Thr
740 745 750
Asp Asp Lys Gly Ala Thr Ala Thr Glu Ser Phe Thr Ile Glu Ile Lys
755 760 765
Asn Glu Asp Thr Thr Thr Pro Ile Thr Lys Glu Met Glu Pro Asn Asp
770 775 780 785
Asp Ile Lys Glu Ala Asn Gly Pro Ile Val Glu Gly Val Thr Val Lys
790 795 800
Gly Asp Leu Asn Gly Ser Asp Asp Ala Asp Thr Phe Tyr Phe Asp Val
805 810 815
Lys Glu Asp Gly Asp Val Thr Ile Glu Leu Pro Tyr Ser Gly Ser Ser
820 825 830
Asn Phe Thr Trp Leu Val Tyr Lys Glu Gly Asp Asp Gln Asn His Ile
835 840 845
Ala Ser Gly Ile Asp Lys Asn Asn Ser Lys Val Gly Thr Phe Lys Ser
850 855 860 865
Thr Lys Gly Arg His Tyr Val Phe Ile Tyr Lys His Asp Ser Ala Ser
870 875 880
Asn Ile Ser Tyr Ser Leu Asn Ile Lys Gly Leu Gly Asn Glu Lys Leu
885 890 895
Lys Glu Lys Glu Asn Asn Asp Ser Ser Asp Lys Ala Thr Val Ile Pro
900 905 910
Asn Phe Asn Thr Thr Met Gln Gly Ser Leu Leu Gly Asp Asp Ser Arg
915 920 925
Asp Tyr Tyr Ser Phe Glu Val Lys Glu Glu Gly Glu Val Asn Ile Glu
930 935 940 945
Leu Asp Lys Lys Asp Glu Phe Gly Val Thr Trp Thr Leu His Pro Glu
950 955 960
Ser Asn Ile Asn Asp Arg Ile Thr Tyr Gly Gln Val Asp Gly Asn Lys
965 970 975
Val Ser Asn Lys Val Lys Leu Arg Pro Gly Lys Tyr Tyr Leu Leu Val
980 985 990
Tyr Lys Tyr Ser Gly Ser Gly Asn Tyr Glu Leu Arg Val Ser Arg Lys
995 1000 1005
Leu Ala Ala Ala Leu Glu His His His His His His
1010 1015 1020
<210> 4
<211> 3396
<212> DNA
<213> Clostridium histolyticum
<220>
<221> CDS
<222> (1)..(3396)
<400> 4
atg aaa aaa aat att tta aag att ctt atg gat agt tat tct aaa gaa 48
Met Lys Lys Asn Ile Leu Lys Ile Leu Met Asp Ser Tyr Ser Lys Glu
1 5 10 15
tct aaa att caa act gta cgt agg gtt acg agt gta tca ctt tta gcg 96
Ser Lys Ile Gln Thr Val Arg Arg Val Thr Ser Val Ser Leu Leu Ala
20 25 30
gta tat ctt act atg aat act tca agt tta gtt tta gca aaa cca ata 144
Val Tyr Leu Thr Met Asn Thr Ser Ser Leu Val Leu Ala Lys Pro Ile
35 40 45
gaa aat act aat gat act agt ata aaa aat gtg gag aaa tta aga aat 192
Glu Asn Thr Asn Asp Thr Ser Ile Lys Asn Val Glu Lys Leu Arg Asn
50 55 60
gct cca aat gaa gag aat agt aaa aag gta gaa gat agt aaa aat gat 240
Ala Pro Asn Glu Glu Asn Ser Lys Lys Val Glu Asp Ser Lys Asn Asp
65 70 75 80
aag gta gaa cat gtg aaa aat ata gaa gag gca aag gtt gag caa gtt 288
Lys Val Glu His Val Lys Asn Ile Glu Glu Ala Lys Val Glu Gln Val
85 90 95
gca ccc gaa gta aaa tct aaa tca act tta aga agt gct tct ata gcg 336
Ala Pro Glu Val Lys Ser Lys Ser Thr Leu Arg Ser Ala Ser Ile Ala
100 105 110
aat act aat tct gag aaa tat gat ttt gag tat tta aat ggt ttg agc 384
Asn Thr Asn Ser Glu Lys Tyr Asp Phe Glu Tyr Leu Asn Gly Leu Ser
115 120 125
tat act gaa ctt aca aat tta att aaa aat ata aag tgg aat caa att 432
Tyr Thr Glu Leu Thr Asn Leu Ile Lys Asn Ile Lys Trp Asn Gln Ile
130 135 140
aat ggt tta ttt aat tat agt aca ggt tct caa aag ttc ttt gga gat 480
Asn Gly Leu Phe Asn Tyr Ser Thr Gly Ser Gln Lys Phe Phe Gly Asp
145 150 155 160
aaa aat cgt gta caa gct ata att aat gct tta caa gaa agt gga aga 528
Lys Asn Arg Val Gln Ala Ile Ile Asn Ala Leu Gln Glu Ser Gly Arg
165 170 175
act tac act gca aat gat atg aag ggt ata gaa act ttc act gag gtt 576
Thr Tyr Thr Ala Asn Asp Met Lys Gly Ile Glu Thr Phe Thr Glu Val
180 185 190
tta aga gct ggt ttt tat tta ggg tac tat aat gat ggt tta tct tat 624
Leu Arg Ala Gly Phe Tyr Leu Gly Tyr Tyr Asn Asp Gly Leu Ser Tyr
195 200 205
tta aat gat aga aac ttc caa gat aaa tgt ata cct gca atg att gca 672
Leu Asn Asp Arg Asn Phe Gln Asp Lys Cys Ile Pro Ala Met Ile Ala
210 215 220
att caa aaa aat cct aac ttt aag cta gga act gca gtt caa gat gaa 720
Ile Gln Lys Asn Pro Asn Phe Lys Leu Gly Thr Ala Val Gln Asp Glu
225 230 235 240
gtt ata act tct tta gga aaa cta ata gga aat gct tct gct aat gct 768
Val Ile Thr Ser Leu Gly Lys Leu Ile Gly Asn Ala Ser Ala Asn Ala
245 250 255
gaa gta gtt aat aat tgt gta cca gtt cta aaa caa ttt aga gaa aac 816
Glu Val Val Asn Asn Cys Val Pro Val Leu Lys Gln Phe Arg Glu Asn
260 265 270
tta aat caa tat gct cct gat tac gtt aaa gga aca gct gta aat gaa 864
Leu Asn Gln Tyr Ala Pro Asp Tyr Val Lys Gly Thr Ala Val Asn Glu
275 280 285
tta att aaa ggt att gaa ttc gat ttt tct ggt gct gca tat gaa aaa 912
Leu Ile Lys Gly Ile Glu Phe Asp Phe Ser Gly Ala Ala Tyr Glu Lys
290 295 300
gat gtt aag aca atg cct tgg tat gga aaa att gat cca ttt ata aat 960
Asp Val Lys Thr Met Pro Trp Tyr Gly Lys Ile Asp Pro Phe Ile Asn
305 310 315 320
gaa ctt aag gcc tta ggt cta tat gga aat ata aca agt gca act gag 1008
Glu Leu Lys Ala Leu Gly Leu Tyr Gly Asn Ile Thr Ser Ala Thr Glu
325 330 335
tgg gca tct gat gtt gga ata tac tat tta agt aaa ttc ggt ctt tac 1056
Trp Ala Ser Asp Val Gly Ile Tyr Tyr Leu Ser Lys Phe Gly Leu Tyr
340 345 350
tca act aac cga aat gac ata gta cag tca ctt gaa aag gct gta gat 1104
Ser Thr Asn Arg Asn Asp Ile Val Gln Ser Leu Glu Lys Ala Val Asp
355 360 365
atg tat aag tat ggt aaa ata gcc ttt gta gca atg gag aga ata act 1152
Met Tyr Lys Tyr Gly Lys Ile Ala Phe Val Ala Met Glu Arg Ile Thr
370 375 380
tgg gat tat gat ggg att ggt tct aat ggt aaa aag gtg gat cac gat 1200
Trp Asp Tyr Asp Gly Ile Gly Ser Asn Gly Lys Lys Val Asp His Asp
385 390 395 400
aag ttc tta gat gat gct gaa aaa cat tat ctg cca aag aca tat act 1248
Lys Phe Leu Asp Asp Ala Glu Lys His Tyr Leu Pro Lys Thr Tyr Thr
405 410 415
ttt gat aat gga acc ttt att ata aga gca ggg gat aag gta tcc gaa 1296
Phe Asp Asn Gly Thr Phe Ile Ile Arg Ala Gly Asp Lys Val Ser Glu
420 425 430
gaa aaa ata aaa agg cta tat tgg gca tca aga gaa gtg aag tct caa 1344
Glu Lys Ile Lys Arg Leu Tyr Trp Ala Ser Arg Glu Val Lys Ser Gln
435 440 445
ttc cat aga gta gtt ggc aat gat aaa gct tta gag gtg gga aat gcc 1392
Phe His Arg Val Val Gly Asn Asp Lys Ala Leu Glu Val Gly Asn Ala
450 455 460
gat gat gtt tta act atg aaa ata ttt aat agc cca gaa gaa tat aaa 1440
Asp Asp Val Leu Thr Met Lys Ile Phe Asn Ser Pro Glu Glu Tyr Lys
465 470 475 480
ttt aat acc aat ata aat ggt gta agc act gat aat ggt ggt cta tat 1488
Phe Asn Thr Asn Ile Asn Gly Val Ser Thr Asp Asn Gly Gly Leu Tyr
485 490 495
ata gaa cca aga ggg act ttc tac act tat gag aga aca cct caa caa 1536
Ile Glu Pro Arg Gly Thr Phe Tyr Thr Tyr Glu Arg Thr Pro Gln Gln
500 505 510
agt ata ttt agt ctt gaa gaa ttg ttt aga cat gaa tat act cac tat 1584
Ser Ile Phe Ser Leu Glu Glu Leu Phe Arg His Glu Tyr Thr His Tyr
515 520 525
tta caa gcg aga tat ctt gta gat ggt tta tgg ggg caa ggt cca ttt 1632
Leu Gln Ala Arg Tyr Leu Val Asp Gly Leu Trp Gly Gln Gly Pro Phe
530 535 540
tat gaa aaa aat aga tta act tgg ttt gat gaa ggt aca gct gaa ttc 1680
Tyr Glu Lys Asn Arg Leu Thr Trp Phe Asp Glu Gly Thr Ala Glu Phe
545 550 555 560
ttt gca gga tct acc cgt aca tct ggt gtt tta cca aga aaa tca ata 1728
Phe Ala Gly Ser Thr Arg Thr Ser Gly Val Leu Pro Arg Lys Ser Ile
565 570 575
tta gga tat ttg gct aag gat aaa gta gat cat aga tac tca tta aag 1776
Leu Gly Tyr Leu Ala Lys Asp Lys Val Asp His Arg Tyr Ser Leu Lys
580 585 590
aag act ctt aat tca ggg tat gat gac agt gat tgg atg ttc tat aat 1824
Lys Thr Leu Asn Ser Gly Tyr Asp Asp Ser Asp Trp Met Phe Tyr Asn
595 600 605
tat gga ttt gca gtt gca cat tac cta tat gaa aaa gat atg cct aca 1872
Tyr Gly Phe Ala Val Ala His Tyr Leu Tyr Glu Lys Asp Met Pro Thr
610 615 620
ttt att aag atg aat aaa gct ata ttg aat aca gat gtg aaa tct tat 1920
Phe Ile Lys Met Asn Lys Ala Ile Leu Asn Thr Asp Val Lys Ser Tyr
625 630 635 640
gat gaa ata ata aaa aaa tta agt gat gat gca aat aaa aat aca gaa 1968
Asp Glu Ile Ile Lys Lys Leu Ser Asp Asp Ala Asn Lys Asn Thr Glu
645 650 655
tat caa aac cat att caa gag tta gca gat aaa tat caa gga gca ggc 2016
Tyr Gln Asn His Ile Gln Glu Leu Ala Asp Lys Tyr Gln Gly Ala Gly
660 665 670
ata cct cta gta tca gat gat tac tta aaa gat cat gga tat aag aaa 2064
Ile Pro Leu Val Ser Asp Asp Tyr Leu Lys Asp His Gly Tyr Lys Lys
675 680 685
gca tct gaa gta tat tct gaa att tca aaa gct gct tct ctt aca aac 2112
Ala Ser Glu Val Tyr Ser Glu Ile Ser Lys Ala Ala Ser Leu Thr Asn
690 695 700
act agt gta aca gca gaa aaa tct caa tat ttt aac aca ttc act tta 2160
Thr Ser Val Thr Ala Glu Lys Ser Gln Tyr Phe Asn Thr Phe Thr Leu
705 710 715 720
aga gga act tat aca ggt gaa act tct aaa ggt gaa ttt aaa gat tgg 2208
Arg Gly Thr Tyr Thr Gly Glu Thr Ser Lys Gly Glu Phe Lys Asp Trp
725 730 735
gat gaa atg agt aaa aaa tta gat gga act ttg gag tcc ctt gct aaa 2256
Asp Glu Met Ser Lys Lys Leu Asp Gly Thr Leu Glu Ser Leu Ala Lys
740 745 750
aat tct tgg agt gga tac aaa act tta aca gca tac ttt acg aat tat 2304
Asn Ser Trp Ser Gly Tyr Lys Thr Leu Thr Ala Tyr Phe Thr Asn Tyr
755 760 765
aga gtt aca agc gat aat aaa gtt caa tat gat gta gtt ttc cat ggg 2352
Arg Val Thr Ser Asp Asn Lys Val Gln Tyr Asp Val Val Phe His Gly
770 775 780
gtt tta aca gat aat gcg gat att agt aac aat aag gct cca ata gca 2400
Val Leu Thr Asp Asn Ala Asp Ile Ser Asn Asn Lys Ala Pro Ile Ala
785 790 795 800
aag gta act gga cca agc act ggt gct gta gga aga aat att gaa ttt 2448
Lys Val Thr Gly Pro Ser Thr Gly Ala Val Gly Arg Asn Ile Glu Phe
805 810 815
agt gga aaa gat agt aaa gat gaa gat ggt aaa ata gta tca tat gat 2496
Ser Gly Lys Asp Ser Lys Asp Glu Asp Gly Lys Ile Val Ser Tyr Asp
820 825 830
tgg gat ttt ggc gat ggt gca act agt aga ggc aaa aat tca gta cat 2544
Trp Asp Phe Gly Asp Gly Ala Thr Ser Arg Gly Lys Asn Ser Val His
835 840 845
gct tac aaa aaa gca gga aca tat aat gtt aca tta aaa gta act gac 2592
Ala Tyr Lys Lys Ala Gly Thr Tyr Asn Val Thr Leu Lys Val Thr Asp
850 855 860
gat aag ggt gca aca gct aca gaa agc ttt act ata gaa ata aag aac 2640
Asp Lys Gly Ala Thr Ala Thr Glu Ser Phe Thr Ile Glu Ile Lys Asn
865 870 875 880
gaa gat aca aca aca cct ata act aaa gaa atg gaa cct aat gat gat 2688
Glu Asp Thr Thr Thr Pro Ile Thr Lys Glu Met Glu Pro Asn Asp Asp
885 890 895
ata aaa gag gct aat ggt cca ata gtt gaa ggt gtt act gta aaa ggt 2736
Ile Lys Glu Ala Asn Gly Pro Ile Val Glu Gly Val Thr Val Lys Gly
900 905 910
gat tta aat ggt tct gat gat gct gat acc ttc tat ttt gat gta aaa 2784
Asp Leu Asn Gly Ser Asp Asp Ala Asp Thr Phe Tyr Phe Asp Val Lys
915 920 925
gaa gat ggt gat gtt aca att gaa ctt cct tat tca ggg tca tct aat 2832
Glu Asp Gly Asp Val Thr Ile Glu Leu Pro Tyr Ser Gly Ser Ser Asn
930 935 940
ttc aca tgg tta gtt tat aaa gag gga gac gat caa aac cat att gca 2880
Phe Thr Trp Leu Val Tyr Lys Glu Gly Asp Asp Gln Asn His Ile Ala
945 950 955 960
agt ggt ata gat aag aat aac tca aaa gtt gga aca ttt aaa tct aca 2928
Ser Gly Ile Asp Lys Asn Asn Ser Lys Val Gly Thr Phe Lys Ser Thr
965 970 975
aaa gga aga cat tat gtg ttt ata tat aaa cac gat tct gct tca aat 2976
Lys Gly Arg His Tyr Val Phe Ile Tyr Lys His Asp Ser Ala Ser Asn
980 985 990
ata tcc tat tct tta aac ata aaa gga tta ggt aac gag aaa ttg aag 3024
Ile Ser Tyr Ser Leu Asn Ile Lys Gly Leu Gly Asn Glu Lys Leu Lys
995 1000 1005
gaa aaa gaa aat aat gat tct tct gat aaa gct aca gtt ata cca 3069
Glu Lys Glu Asn Asn Asp Ser Ser Asp Lys Ala Thr Val Ile Pro
1010 1015 1020
aat ttc aat acc act atg caa ggt tca ctt tta ggt gat gat tca 3114
Asn Phe Asn Thr Thr Met Gln Gly Ser Leu Leu Gly Asp Asp Ser
1025 1030 1035
aga gat tat tat tct ttt gag gtt aag gaa gaa ggc gaa gtt aat 3159
Arg Asp Tyr Tyr Ser Phe Glu Val Lys Glu Glu Gly Glu Val Asn
1040 1045 1050
ata gaa cta gat aaa aag gat gaa ttt ggt gta aca tgg aca cta 3204
Ile Glu Leu Asp Lys Lys Asp Glu Phe Gly Val Thr Trp Thr Leu
1055 1060 1065
cat cca gag tca aat att aat gac aga ata act tac gga caa gtt 3249
His Pro Glu Ser Asn Ile Asn Asp Arg Ile Thr Tyr Gly Gln Val
1070 1075 1080
gat ggt aat aag gta tct aat aaa gtt aaa tta aga cca gga aaa 3294
Asp Gly Asn Lys Val Ser Asn Lys Val Lys Leu Arg Pro Gly Lys
1085 1090 1095
tat tat cta ctt gtt tat aaa tac tca gga tca gga aac tat gag 3339
Tyr Tyr Leu Leu Val Tyr Lys Tyr Ser Gly Ser Gly Asn Tyr Glu
1100 1105 1110
tta agg gta tct aga aag ctt gcg gcc gca ctc gag cac cac cac 3384
Leu Arg Val Ser Arg Lys Leu Ala Ala Ala Leu Glu His His His
1115 1120 1125
cac cac cac tga 3396
His His His
1130
<210> 5
<211> 1021
<212> PRT
<213> Clostridium histolyticum
<220>
<221> SIGNAL
<222> (-40)..(-1)
<220>
<221> mat_peptide
<222> (1)..(981)
<400> 5
Met Lys Arg Lys Cys Leu Ser Lys Arg Leu Met Leu Ala Ile Thr Met
-40 -35 -30 -25
Ala Thr Ile Phe Thr Val Asn Ser Thr Leu Pro Ile Tyr Ala Ala Val
-20 -15 -10
Asp Lys Asn Asn Ala Thr Ala Ala Val Gln Asn Glu Ser Lys Arg Tyr
-5 -1 1 5
Thr Val Ser Tyr Leu Lys Thr Leu Asn Tyr Tyr Asp Leu Val Asp Leu
10 15 20
Leu Val Lys Thr Glu Ile Glu Asn Leu Pro Asp Leu Phe Gln Tyr Ser
25 30 35 40
Ser Asp Ala Lys Glu Phe Tyr Gly Asn Lys Thr Arg Met Ser Phe Ile
45 50 55
Met Asp Glu Ile Gly Arg Arg Ala Pro Gln Tyr Thr Glu Ile Asp His
60 65 70
Lys Gly Ile Pro Thr Leu Val Glu Val Val Arg Ala Gly Phe Tyr Leu
75 80 85
Gly Phe His Asn Lys Glu Leu Asn Glu Ile Asn Lys Arg Ser Phe Lys
90 95 100
Glu Arg Val Ile Pro Ser Ile Leu Ala Ile Gln Lys Asn Pro Asn Phe
105 110 115 120
Lys Leu Gly Thr Glu Val Gln Asp Lys Ile Val Ser Ala Thr Gly Leu
125 130 135
Leu Ala Gly Asn Glu Thr Ala Pro Pro Glu Val Val Asn Asn Phe Thr
140 145 150
Pro Ile Leu Gln Asp Cys Ile Lys Asn Ile Asp Arg Tyr Ala Leu Asp
155 160 165
Asp Leu Lys Ser Lys Ala Leu Phe Asn Val Leu Ala Ala Pro Thr Tyr
170 175 180
Asp Ile Thr Glu Tyr Leu Arg Ala Thr Lys Glu Lys Pro Glu Asn Thr
185 190 195 200
Pro Trp Tyr Gly Lys Ile Asp Gly Phe Ile Asn Glu Leu Lys Lys Leu
205 210 215
Ala Leu Tyr Gly Lys Ile Asn Asp Asn Asn Ser Trp Ile Ile Asp Asn
220 225 230
Gly Ile Tyr His Ile Ala Pro Leu Gly Lys Leu His Ser Asn Asn Lys
235 240 245
Ile Gly Ile Glu Thr Leu Thr Glu Val Met Lys Val Tyr Pro Tyr Leu
250 255 260
Ser Met Gln His Leu Gln Ser Ala Asp Gln Ile Lys Arg His Tyr Asp
265 270 275 280
Ser Lys Asp Ala Glu Gly Asn Lys Ile Pro Leu Asp Lys Phe Lys Lys
285 290 295
Glu Gly Lys Glu Lys Tyr Cys Pro Lys Thr Tyr Thr Phe Asp Asp Gly
300 305 310
Lys Val Ile Ile Lys Ala Gly Ala Arg Val Glu Glu Glu Lys Val Lys
315 320 325
Arg Leu Tyr Trp Ala Ser Lys Glu Val Asn Ser Gln Phe Phe Arg Val
330 335 340
Tyr Gly Ile Asp Lys Pro Leu Glu Glu Gly Asn Pro Asp Asp Ile Leu
345 350 355 360
Thr Met Val Ile Tyr Asn Ser Pro Glu Glu Tyr Lys Leu Asn Ser Val
365 370 375
Leu Tyr Gly Tyr Asp Thr Asn Asn Gly Gly Met Tyr Ile Glu Pro Glu
380 385 390
Gly Thr Phe Phe Thr Tyr Glu Arg Glu Ala Gln Glu Ser Thr Tyr Thr
395 400 405
Leu Glu Glu Leu Phe Arg His Glu Tyr Thr His Tyr Leu Gln Gly Arg
410 415 420
Tyr Ala Val Pro Gly Gln Trp Gly Arg Thr Lys Leu Tyr Asp Asn Asp
425 430 435 440
Arg Leu Thr Trp Tyr Glu Glu Gly Gly Ala Glu Leu Phe Ala Gly Ser
445 450 455
Thr Arg Thr Ser Gly Ile Leu Pro Arg Lys Ser Ile Val Ser Asn Ile
460 465 470
His Asn Thr Thr Arg Asn Asn Arg Tyr Lys Leu Ser Asp Thr Val His
475 480 485
Ser Lys Tyr Gly Ala Ser Phe Glu Phe Tyr Asn Tyr Ala Cys Met Phe
490 495 500
Met Asp Tyr Met Tyr Asn Lys Asp Met Gly Ile Leu Asn Lys Leu Asn
505 510 515 520
Asp Leu Ala Lys Asn Asn Asp Val Asp Gly Tyr Asp Asn Tyr Ile Arg
525 530 535
Asp Leu Ser Ser Asn Tyr Ala Leu Asn Asp Lys Tyr Gln Asp His Met
540 545 550
Gln Glu Arg Ile Asp Asn Tyr Glu Asn Leu Thr Val Pro Phe Val Ala
555 560 565
Asp Asp Tyr Leu Val Arg His Ala Tyr Lys Asn Pro Asn Glu Ile Tyr
570 575 580
Ser Glu Ile Ser Glu Val Ala Lys Leu Lys Asp Ala Lys Ser Glu Val
585 590 595 600
Lys Lys Ser Gln Tyr Phe Ser Thr Phe Thr Leu Arg Gly Ser Tyr Thr
605 610 615
Gly Gly Ala Ser Lys Gly Lys Leu Glu Asp Gln Lys Ala Met Asn Lys
620 625 630
Phe Ile Asp Asp Ser Leu Lys Lys Leu Asp Thr Tyr Ser Trp Ser Gly
635 640 645
Tyr Lys Thr Leu Thr Ala Tyr Phe Thr Asn Tyr Lys Val Asp Ser Ser
650 655 660
Asn Arg Val Thr Tyr Asp Val Val Phe His Gly Tyr Leu Pro Asn Glu
665 670 675 680
Gly Asp Ser Lys Asn Ser Leu Pro Tyr Gly Lys Ile Asn Gly Thr Tyr
685 690 695
Lys Gly Thr Glu Lys Glu Lys Ile Lys Phe Ser Ser Glu Gly Ser Phe
700 705 710
Asp Pro Asp Gly Lys Ile Val Ser Tyr Glu Trp Asp Phe Gly Asp Gly
715 720 725
Asn Lys Ser Asn Glu Glu Asn Pro Glu His Ser Tyr Asp Lys Val Gly
730 735 740
Thr Tyr Thr Val Lys Leu Lys Val Thr Asp Asp Lys Gly Glu Ser Ser
745 750 755 760
Val Ser Thr Thr Thr Ala Glu Ile Lys Asp Leu Ser Glu Asn Lys Leu
765 770 775
Pro Val Ile Tyr Met His Val Pro Lys Ser Gly Ala Leu Asn Gln Lys
780 785 790
Val Val Phe Tyr Gly Lys Gly Thr Tyr Asp Pro Asp Gly Ser Ile Ala
795 800 805
Gly Tyr Gln Trp Asp Phe Gly Asp Gly Ser Asp Phe Ser Ser Glu Gln
810 815 820
Asn Pro Ser His Val Tyr Thr Lys Lys Gly Glu Tyr Thr Val Thr Leu
825 830 835 840
Arg Val Met Asp Ser Ser Gly Gln Met Ser Glu Lys Thr Met Lys Ile
845 850 855
Lys Ile Thr Asp Pro Val Tyr Pro Ile Gly Thr Glu Lys Glu Pro Asn
860 865 870
Asn Ser Lys Glu Thr Ala Ser Gly Pro Ile Val Pro Gly Ile Pro Val
875 880 885
Ser Gly Thr Ile Glu Asn Thr Ser Asp Gln Asp Tyr Phe Tyr Phe Asp
890 895 900
Val Ile Thr Pro Gly Glu Val Lys Ile Asp Ile Asn Lys Leu Gly Tyr
905 910 915 920
Gly Gly Ala Thr Trp Val Val Tyr Asp Glu Asn Asn Asn Ala Val Ser
925 930 935
Tyr Ala Thr Asp Asp Gly Gln Asn Leu Ser Gly Lys Phe Lys Ala Asp
940 945 950
Lys Pro Gly Arg Tyr Tyr Ile His Leu Tyr Met Phe Asn Gly Ser Tyr
955 960 965
Met Pro Tyr Arg Ile Asn Ile Glu Gly Ser Val Gly Arg
970 975 980
<210> 6
<211> 1021
<212> PRT
<213> Clostridium histolyticum
<220>
<221> SIGNAL
<222> (-40)..(-1)
<220>
<221> mat_peptide
<222> (1)..(981)
<400> 6
Met Lys Arg Lys Cys Leu Ser Lys Arg Leu Met Leu Ala Ile Thr Met
-40 -35 -30 -25
Ala Thr Ile Phe Thr Val Asn Ser Thr Leu Pro Ile Tyr Ala Ala Val
-20 -15 -10
Asp Lys Asn Asn Ala Thr Ala Ala Val Gln Asn Glu Ser Lys Arg Tyr
-5 -1 1 5
Thr Val Ser Tyr Leu Lys Thr Leu Asn Tyr Tyr Asp Leu Val Asp Leu
10 15 20
Leu Val Lys Thr Glu Ile Glu Asn Leu Pro Asp Leu Phe Gln Tyr Ser
25 30 35 40
Ser Asp Ala Lys Glu Phe Tyr Gly Asn Lys Thr Arg Met Ser Phe Ile
45 50 55
Met Asp Glu Ile Gly Arg Arg Ala Pro Gln Tyr Thr Glu Ile Asp His
60 65 70
Lys Gly Ile Pro Thr Leu Val Glu Val Val Arg Ala Gly Phe Tyr Leu
75 80 85
Gly Phe His Asn Lys Glu Leu Asn Glu Ile Asn Lys Arg Ser Phe Lys
90 95 100
Glu Arg Val Ile Pro Ser Ile Leu Ala Ile Gln Lys Asn Pro Asn Phe
105 110 115 120
Lys Leu Gly Thr Glu Val Gln Asp Lys Ile Val Ser Ala Thr Gly Leu
125 130 135
Leu Ala Gly Asn Glu Thr Ala Pro Pro Glu Val Val Asn Asn Phe Thr
140 145 150
Pro Ile Leu Gln Asp Cys Ile Lys Asn Ile Asp Arg Tyr Ala Leu Asp
155 160 165
Asp Leu Lys Ser Lys Ala Leu Phe Asn Val Leu Ala Ala Pro Thr Tyr
170 175 180
Asp Ile Thr Glu Tyr Leu Arg Ala Thr Lys Glu Lys Pro Glu Asn Thr
185 190 195 200
Pro Trp Tyr Gly Lys Ile Asp Gly Phe Ile Asn Glu Leu Lys Lys Leu
205 210 215
Ala Leu Tyr Gly Lys Ile Asn Asp Asn Asn Ser Trp Ile Ile Asp Asn
220 225 230
Gly Ile Tyr His Ile Ala Pro Leu Gly Lys Leu His Ser Asn Asn Lys
235 240 245
Ile Gly Ile Glu Thr Leu Thr Glu Val Met Lys Val Tyr Pro Tyr Leu
250 255 260
Ser Met Gln His Leu Gln Ser Ala Asp Gln Ile Lys Arg His Tyr Asp
265 270 275 280
Ser Lys Asp Ala Glu Gly Asn Lys Ile Pro Leu Asp Lys Phe Lys Lys
285 290 295
Glu Gly Lys Glu Lys Tyr Cys Pro Lys Thr Tyr Thr Phe Asp Asp Gly
300 305 310
Lys Val Ile Ile Lys Ala Gly Ala Arg Val Glu Glu Glu Lys Val Lys
315 320 325
Arg Leu Tyr Trp Ala Ser Lys Glu Val Asn Ser Gln Phe Phe Arg Val
330 335 340
Tyr Gly Ile Asp Lys Pro Leu Glu Glu Gly Asn Pro Asp Asp Ile Leu
345 350 355 360
Thr Met Val Ile Tyr Asn Ser Pro Glu Glu Tyr Lys Leu Asn Ser Val
365 370 375
Leu Tyr Gly Tyr Asp Thr Asn Asn Gly Gly Met Tyr Ile Glu Pro Glu
380 385 390
Gly Thr Phe Phe Thr Tyr Glu Arg Glu Ala Gln Glu Ser Thr Tyr Thr
395 400 405
Leu Glu Glu Leu Phe Arg His Glu Tyr Thr His Tyr Leu Gln Gly Arg
410 415 420
Tyr Ala Val Pro Gly Gln Trp Gly Arg Thr Lys Leu Tyr Asp Asn Asp
425 430 435 440
Arg Leu Thr Trp Tyr Glu Glu Gly Gly Ala Glu Leu Phe Ala Gly Ser
445 450 455
Thr Arg Thr Ser Gly Ile Leu Pro Arg Lys Ser Ile Val Ser Asn Ile
460 465 470
His Asn Thr Thr Arg Asn Asn Arg Tyr Lys Leu Ser Asp Thr Val His
475 480 485
Ser Lys Tyr Gly Ala Ser Phe Glu Phe Tyr Asn Tyr Ala Cys Met Phe
490 495 500
Met Asp Tyr Met Tyr Asn Lys Asp Met Gly Ile Leu Asn Lys Leu Asn
505 510 515 520
Asp Leu Ala Lys Asn Asn Asp Val Asp Gly Tyr Asp Asn Tyr Ile Arg
525 530 535
Asp Leu Ser Ser Asn Tyr Ala Leu Asn Asp Lys Tyr Gln Asp His Met
540 545 550
Gln Glu Arg Ile Asp Asn Tyr Glu Asn Leu Thr Val Pro Phe Val Ala
555 560 565
Asp Asp Tyr Leu Val Arg His Ala Tyr Lys Asn Pro Asn Glu Ile Tyr
570 575 580
Ser Glu Ile Ser Glu Val Ala Lys Leu Lys Asp Ala Lys Ser Glu Val
585 590 595 600
Lys Lys Ser Gln Tyr Phe Ser Thr Phe Thr Leu Arg Gly Ser Tyr Thr
605 610 615
Gly Gly Ala Ser Lys Gly Lys Leu Glu Asp Gln Lys Ala Met Asn Lys
620 625 630
Phe Ile Asp Asp Ser Leu Lys Lys Leu Asp Thr Tyr Ser Trp Ser Gly
635 640 645
Tyr Lys Thr Leu Thr Ala Tyr Phe Thr Asn Tyr Lys Val Asp Ser Ser
650 655 660
Asn Arg Val Thr Tyr Asp Val Val Phe His Gly Tyr Leu Pro Asn Glu
665 670 675 680
Gly Asp Ser Lys Asn Ser Leu Pro Tyr Gly Lys Ile Asn Gly Thr Tyr
685 690 695
Lys Gly Thr Glu Lys Glu Lys Ile Lys Phe Ser Ser Glu Gly Ser Phe
700 705 710
Asp Pro Asp Gly Lys Ile Val Ser Tyr Glu Trp Asp Phe Gly Asp Gly
715 720 725
Asn Lys Ser Asn Glu Glu Asn Pro Glu His Ser Tyr Asp Lys Val Gly
730 735 740
Thr Tyr Thr Val Lys Leu Lys Val Thr Asp Asp Lys Gly Glu Ser Ser
745 750 755 760
Val Ser Thr Thr Thr Ala Glu Ile Lys Asp Leu Ser Glu Asn Lys Leu
765 770 775
Pro Val Ile Tyr Met His Val Pro Lys Ser Gly Ala Leu Asn Gln Lys
780 785 790
Val Val Phe Tyr Gly Lys Gly Thr Tyr Asp Pro Asp Gly Ser Ile Ala
795 800 805
Gly Tyr Gln Trp Asp Phe Gly Asp Gly Ser Asp Phe Ser Ser Glu Gln
810 815 820
Asn Pro Ser His Val Tyr Thr Lys Lys Gly Glu Tyr Thr Val Thr Leu
825 830 835 840
Arg Val Met Asp Ser Ser Gly Gln Met Ser Glu Lys Thr Met Lys Ile
845 850 855
Lys Ile Thr Asp Pro Val Tyr Pro Ile Gly Thr Glu Lys Glu Pro Asn
860 865 870
Asn Ser Lys Glu Thr Ala Ser Gly Pro Ile Val Pro Gly Ile Pro Val
875 880 885
Ser Gly Thr Ile Glu Asn Thr Ser Asp Gln Asp Tyr Phe Tyr Phe Asp
890 895 900
Val Ile Thr Pro Gly Glu Val Lys Ile Asp Ile Asn Lys Leu Gly Tyr
905 910 915 920
Gly Gly Ala Thr Trp Val Val Tyr Asp Glu Asn Asn Asn Ala Val Ser
925 930 935
Tyr Ala Thr Asp Asp Gly Gln Asn Leu Ser Gly Lys Phe Lys Ala Asp
940 945 950
Lys Pro Gly Arg Tyr Tyr Ile His Leu Tyr Met Phe Asn Gly Ser Tyr
955 960 965
Met Pro Tyr Arg Ile Asn Ile Glu Gly Ser Val Ser Arg
970 975 980
<210> 7
<211> 1034
<212> PRT
<213> Clostridium histolyticum
<220>
<221> SIGNAL
<222> (-40)..(-1)
<220>
<221> mat_peptide
<222> (1)..(994)
<400> 7
Met Lys Arg Lys Cys Leu Ser Lys Arg Leu Met Leu Ala Ile Thr Met
-40 -35 -30 -25
Ala Thr Ile Phe Thr Val Asn Ser Thr Leu Pro Ile Tyr Ala Ala Val
-20 -15 -10
Asp Lys Asn Asn Ala Thr Ala Ala Val Gln Asn Glu Ser Lys Arg Tyr
-5 -1 1 5
Thr Val Ser Tyr Leu Lys Thr Leu Asn Tyr Tyr Asp Leu Val Asp Leu
10 15 20
Leu Val Lys Thr Glu Ile Glu Asn Leu Pro Asp Leu Phe Gln Tyr Ser
25 30 35 40
Ser Asp Ala Lys Glu Phe Tyr Gly Asn Lys Thr Arg Met Ser Phe Ile
45 50 55
Met Asp Glu Ile Gly Arg Arg Ala Pro Gln Tyr Thr Glu Ile Asp His
60 65 70
Lys Gly Ile Pro Thr Leu Val Glu Val Val Arg Ala Gly Phe Tyr Leu
75 80 85
Gly Phe His Asn Lys Glu Leu Asn Glu Ile Asn Lys Arg Ser Phe Lys
90 95 100
Glu Arg Val Ile Pro Ser Ile Leu Ala Ile Gln Lys Asn Pro Asn Phe
105 110 115 120
Lys Leu Gly Thr Glu Val Gln Asp Lys Ile Val Ser Ala Thr Gly Leu
125 130 135
Leu Ala Gly Asn Glu Thr Ala Pro Pro Glu Val Val Asn Asn Phe Thr
140 145 150
Pro Ile Leu Gln Asp Cys Ile Lys Asn Ile Asp Arg Tyr Ala Leu Asp
155 160 165
Asp Leu Lys Ser Lys Ala Leu Phe Asn Val Leu Ala Ala Pro Thr Tyr
170 175 180
Asp Ile Thr Glu Tyr Leu Arg Ala Thr Lys Glu Lys Pro Glu Asn Thr
185 190 195 200
Pro Trp Tyr Gly Lys Ile Asp Gly Phe Ile Asn Glu Leu Lys Lys Leu
205 210 215
Ala Leu Tyr Gly Lys Ile Asn Asp Asn Asn Ser Trp Ile Ile Asp Asn
220 225 230
Gly Ile Tyr His Ile Ala Pro Leu Gly Lys Leu His Ser Asn Asn Lys
235 240 245
Ile Gly Ile Glu Thr Leu Thr Glu Val Met Lys Val Tyr Pro Tyr Leu
250 255 260
Ser Met Gln His Leu Gln Ser Ala Asp Gln Ile Lys Arg His Tyr Asp
265 270 275 280
Ser Lys Asp Ala Glu Gly Asn Lys Ile Pro Leu Asp Lys Phe Lys Lys
285 290 295
Glu Gly Lys Glu Lys Tyr Cys Pro Lys Thr Tyr Thr Phe Asp Asp Gly
300 305 310
Lys Val Ile Ile Lys Ala Gly Ala Arg Val Glu Glu Glu Lys Val Lys
315 320 325
Arg Leu Tyr Trp Ala Ser Lys Glu Val Asn Ser Gln Phe Phe Arg Val
330 335 340
Tyr Gly Ile Asp Lys Pro Leu Glu Glu Gly Asn Pro Asp Asp Ile Leu
345 350 355 360
Thr Met Val Ile Tyr Asn Ser Pro Glu Glu Tyr Lys Leu Asn Ser Val
365 370 375
Leu Tyr Gly Tyr Asp Thr Asn Asn Gly Gly Met Tyr Ile Glu Pro Glu
380 385 390
Gly Thr Phe Phe Thr Tyr Glu Arg Glu Ala Gln Glu Ser Thr Tyr Thr
395 400 405
Leu Glu Glu Leu Phe Arg His Glu Tyr Thr His Tyr Leu Gln Gly Arg
410 415 420
Tyr Ala Val Pro Gly Gln Trp Gly Arg Thr Lys Leu Tyr Asp Asn Asp
425 430 435 440
Arg Leu Thr Trp Tyr Glu Glu Gly Gly Ala Glu Leu Phe Ala Gly Ser
445 450 455
Thr Arg Thr Ser Gly Ile Leu Pro Arg Lys Ser Ile Val Ser Asn Ile
460 465 470
His Asn Thr Thr Arg Asn Asn Arg Tyr Lys Leu Ser Asp Thr Val His
475 480 485
Ser Lys Tyr Gly Ala Ser Phe Glu Phe Tyr Asn Tyr Ala Cys Met Phe
490 495 500
Met Asp Tyr Met Tyr Asn Lys Asp Met Gly Ile Leu Asn Lys Leu Asn
505 510 515 520
Asp Leu Ala Lys Asn Asn Asp Val Asp Gly Tyr Asp Asn Tyr Ile Arg
525 530 535
Asp Leu Ser Ser Asn Tyr Ala Leu Asn Asp Lys Tyr Gln Asp His Met
540 545 550
Gln Glu Arg Ile Asp Asn Tyr Glu Asn Leu Thr Val Pro Phe Val Ala
555 560 565
Asp Asp Tyr Leu Val Arg His Ala Tyr Lys Asn Pro Asn Glu Ile Tyr
570 575 580
Ser Glu Ile Ser Glu Val Ala Lys Leu Lys Asp Ala Lys Ser Glu Val
585 590 595 600
Lys Lys Ser Gln Tyr Phe Ser Thr Phe Thr Leu Arg Gly Ser Tyr Thr
605 610 615
Gly Gly Ala Ser Lys Gly Lys Leu Glu Asp Gln Lys Ala Met Asn Lys
620 625 630
Phe Ile Asp Asp Ser Leu Lys Lys Leu Asp Thr Tyr Ser Trp Ser Gly
635 640 645
Tyr Lys Thr Leu Thr Ala Tyr Phe Thr Asn Tyr Lys Val Asp Ser Ser
650 655 660
Asn Arg Val Thr Tyr Asp Val Val Phe His Gly Tyr Leu Pro Asn Glu
665 670 675 680
Gly Asp Ser Lys Asn Ser Leu Pro Tyr Gly Lys Ile Asn Gly Thr Tyr
685 690 695
Lys Gly Thr Glu Lys Glu Lys Ile Lys Phe Ser Ser Glu Gly Ser Phe
700 705 710
Asp Pro Asp Gly Lys Ile Val Ser Tyr Glu Trp Asp Phe Gly Asp Gly
715 720 725
Asn Lys Ser Asn Glu Glu Asn Pro Glu His Ser Tyr Asp Lys Val Gly
730 735 740
Thr Tyr Thr Val Lys Leu Lys Val Thr Asp Asp Lys Gly Glu Ser Ser
745 750 755 760
Val Ser Thr Thr Thr Ala Glu Ile Lys Asp Leu Ser Glu Asn Lys Leu
765 770 775
Pro Val Ile Tyr Met His Val Pro Lys Ser Gly Ala Leu Asn Gln Lys
780 785 790
Val Val Phe Tyr Gly Lys Gly Thr Tyr Asp Pro Asp Gly Ser Ile Ala
795 800 805
Gly Tyr Gln Trp Asp Phe Gly Asp Gly Ser Asp Phe Ser Ser Glu Gln
810 815 820
Asn Pro Ser His Val Tyr Thr Lys Lys Gly Glu Tyr Thr Val Thr Leu
825 830 835 840
Arg Val Met Asp Ser Ser Gly Gln Met Ser Glu Lys Thr Met Lys Ile
845 850 855
Lys Ile Thr Asp Pro Val Tyr Pro Ile Gly Thr Glu Lys Glu Pro Asn
860 865 870
Asn Ser Lys Glu Thr Ala Ser Gly Pro Ile Val Pro Gly Ile Pro Val
875 880 885
Ser Gly Thr Ile Glu Asn Thr Ser Asp Gln Asp Tyr Phe Tyr Phe Asp
890 895 900
Val Ile Thr Pro Gly Glu Val Lys Ile Asp Ile Asn Lys Leu Gly Tyr
905 910 915 920
Gly Gly Ala Thr Trp Val Val Tyr Asp Glu Asn Asn Asn Ala Val Ser
925 930 935
Tyr Ala Thr Asp Asp Gly Gln Asn Leu Ser Gly Lys Phe Lys Ala Asp
940 945 950
Lys Pro Gly Arg Tyr Tyr Ile His Leu Tyr Met Phe Asn Gly Ser Tyr
955 960 965
Met Pro Tyr Arg Ile Asn Ile Glu Gly Ser Val Ser Arg Lys Leu Ala
970 975 980
Ala Ala Leu Glu His His His His His His
985 990
<210> 8
<211> 3105
<212> DNA
<213> Clostridium histolyticum
<220>
<221> CDS
<222> (1)..(3105)
<400> 8
atg aaa agg aaa tgt tta tct aaa agg ctt atg tta gct ata aca atg 48
Met Lys Arg Lys Cys Leu Ser Lys Arg Leu Met Leu Ala Ile Thr Met
1 5 10 15
gct aca ata ttt aca gtg aac agt aca tta cca att tat gca gct gta 96
Ala Thr Ile Phe Thr Val Asn Ser Thr Leu Pro Ile Tyr Ala Ala Val
20 25 30
gat aaa aat aat gca aca gca gct gta caa aat gaa agt aag agg tat 144
Asp Lys Asn Asn Ala Thr Ala Ala Val Gln Asn Glu Ser Lys Arg Tyr
35 40 45
aca gta tca tat tta aag act tta aat tat tat gac tta gta gat ttg 192
Thr Val Ser Tyr Leu Lys Thr Leu Asn Tyr Tyr Asp Leu Val Asp Leu
50 55 60
ctt gtt aag act gaa att gag aat tta cca gac ctt ttt cag tat agt 240
Leu Val Lys Thr Glu Ile Glu Asn Leu Pro Asp Leu Phe Gln Tyr Ser
65 70 75 80
tca gat gca aaa gag ttc tat gga aat aaa act cgt atg agc ttt atc 288
Ser Asp Ala Lys Glu Phe Tyr Gly Asn Lys Thr Arg Met Ser Phe Ile
85 90 95
atg gat gaa att ggt aga agg gca cct cag tat aca gag ata gat cat 336
Met Asp Glu Ile Gly Arg Arg Ala Pro Gln Tyr Thr Glu Ile Asp His
100 105 110
aaa ggt att cct act tta gta gaa gtt gta aga gct gga ttt tac tta 384
Lys Gly Ile Pro Thr Leu Val Glu Val Val Arg Ala Gly Phe Tyr Leu
115 120 125
gga ttc cat aac aag gaa ttg aat gaa ata aac aag agg tct ttt aaa 432
Gly Phe His Asn Lys Glu Leu Asn Glu Ile Asn Lys Arg Ser Phe Lys
130 135 140
gaa agg gta ata cct tct ata tta gca att caa aaa aat cct aat ttt 480
Glu Arg Val Ile Pro Ser Ile Leu Ala Ile Gln Lys Asn Pro Asn Phe
145 150 155 160
aaa cta ggt act gaa gtt caa gat aaa ata gta tct gca aca gga ctt 528
Lys Leu Gly Thr Glu Val Gln Asp Lys Ile Val Ser Ala Thr Gly Leu
165 170 175
tta gct ggt aat gaa aca gcg cct cca gaa gtt gta aat aat ttt aca 576
Leu Ala Gly Asn Glu Thr Ala Pro Pro Glu Val Val Asn Asn Phe Thr
180 185 190
cca ata ctt caa gac tgt ata aag aat ata gac aga tac gct ctt gat 624
Pro Ile Leu Gln Asp Cys Ile Lys Asn Ile Asp Arg Tyr Ala Leu Asp
195 200 205
gat tta aag tca aaa gca tta ttt aat gtt tta gct gca cct acc tat 672
Asp Leu Lys Ser Lys Ala Leu Phe Asn Val Leu Ala Ala Pro Thr Tyr
210 215 220
gat ata act gag tat tta aga gct act aaa gaa aaa cca gaa aac act 720
Asp Ile Thr Glu Tyr Leu Arg Ala Thr Lys Glu Lys Pro Glu Asn Thr
225 230 235 240
cct tgg tat ggt aaa ata gat ggg ttt ata aat gaa ctt aaa aag tta 768
Pro Trp Tyr Gly Lys Ile Asp Gly Phe Ile Asn Glu Leu Lys Lys Leu
245 250 255
gct ctt tat gga aaa ata aat gat aat aac tct tgg ata ata gat aac 816
Ala Leu Tyr Gly Lys Ile Asn Asp Asn Asn Ser Trp Ile Ile Asp Asn
260 265 270
ggt ata tat cat ata gca cct tta ggg aag tta cat agc aat aat aaa 864
Gly Ile Tyr His Ile Ala Pro Leu Gly Lys Leu His Ser Asn Asn Lys
275 280 285
ata gga ata gaa act tta aca gag gtt atg aaa gtt tat cct tat tta 912
Ile Gly Ile Glu Thr Leu Thr Glu Val Met Lys Val Tyr Pro Tyr Leu
290 295 300
agt atg caa cat tta caa tca gca gat caa att aag cgt cat tat gat 960
Ser Met Gln His Leu Gln Ser Ala Asp Gln Ile Lys Arg His Tyr Asp
305 310 315 320
tca aaa gat gct gaa gga aac aaa ata cct tta gat aag ttt aaa aag 1008
Ser Lys Asp Ala Glu Gly Asn Lys Ile Pro Leu Asp Lys Phe Lys Lys
325 330 335
gaa gga aaa gaa aaa tac tgt cca aaa act tat aca ttt gat gat gga 1056
Glu Gly Lys Glu Lys Tyr Cys Pro Lys Thr Tyr Thr Phe Asp Asp Gly
340 345 350
aaa gta ata ata aaa gct ggt gct aga gta gaa gaa gaa aaa gtt aaa 1104
Lys Val Ile Ile Lys Ala Gly Ala Arg Val Glu Glu Glu Lys Val Lys
355 360 365
aga cta tac tgg gca tca aag gaa gtt aac tct caa ttc ttt aga gta 1152
Arg Leu Tyr Trp Ala Ser Lys Glu Val Asn Ser Gln Phe Phe Arg Val
370 375 380
tac gga ata gac aaa cca tta gaa gaa ggt aat cca gat gat ata tta 1200
Tyr Gly Ile Asp Lys Pro Leu Glu Glu Gly Asn Pro Asp Asp Ile Leu
385 390 395 400
aca atg gtt atc tac aac agt ccc gaa gaa tat aaa ctc aat agt gtt 1248
Thr Met Val Ile Tyr Asn Ser Pro Glu Glu Tyr Lys Leu Asn Ser Val
405 410 415
cta tac gga tat gat act aat aat ggt ggt atg tat ata gag cca gaa 1296
Leu Tyr Gly Tyr Asp Thr Asn Asn Gly Gly Met Tyr Ile Glu Pro Glu
420 425 430
gga act ttc ttc acc tat gaa aga gaa gct caa gaa agc aca tac aca 1344
Gly Thr Phe Phe Thr Tyr Glu Arg Glu Ala Gln Glu Ser Thr Tyr Thr
435 440 445
tta gaa gaa tta ttt aga cat gaa tat aca cat tat ttg caa gga aga 1392
Leu Glu Glu Leu Phe Arg His Glu Tyr Thr His Tyr Leu Gln Gly Arg
450 455 460
tat gca gtt cca gga caa tgg gga aga aca aaa ctt tat gac aat gat 1440
Tyr Ala Val Pro Gly Gln Trp Gly Arg Thr Lys Leu Tyr Asp Asn Asp
465 470 475 480
aga tta act tgg tat gaa gaa ggt gga gca gaa tta ttt gca ggt tct 1488
Arg Leu Thr Trp Tyr Glu Glu Gly Gly Ala Glu Leu Phe Ala Gly Ser
485 490 495
act aga act tct gga ata tta cca aga aag agt ata gta tca aat att 1536
Thr Arg Thr Ser Gly Ile Leu Pro Arg Lys Ser Ile Val Ser Asn Ile
500 505 510
cat aat aca aca aga aat aat aga tat aag ctt tca gac act gta cat 1584
His Asn Thr Thr Arg Asn Asn Arg Tyr Lys Leu Ser Asp Thr Val His
515 520 525
tct aaa tat ggt gct agt ttt gaa ttc tat aat tat gca tgt atg ttt 1632
Ser Lys Tyr Gly Ala Ser Phe Glu Phe Tyr Asn Tyr Ala Cys Met Phe
530 535 540
atg gat tat atg tat aat aaa gat atg ggt ata tta aat aaa cta aat 1680
Met Asp Tyr Met Tyr Asn Lys Asp Met Gly Ile Leu Asn Lys Leu Asn
545 550 555 560
gat ctt gca aaa aat aat gat gtt gat gga tat gat aat tat att aga 1728
Asp Leu Ala Lys Asn Asn Asp Val Asp Gly Tyr Asp Asn Tyr Ile Arg
565 570 575
gat tta agt tct aat tat gct tta aat gat aaa tat caa gat cat atg 1776
Asp Leu Ser Ser Asn Tyr Ala Leu Asn Asp Lys Tyr Gln Asp His Met
580 585 590
cag gag cgc ata gat aat tat gaa aat tta aca gtg cct ttt gta gct 1824
Gln Glu Arg Ile Asp Asn Tyr Glu Asn Leu Thr Val Pro Phe Val Ala
595 600 605
gat gat tat tta gta agg cat gct tat aag aac cct aat gaa att tat 1872
Asp Asp Tyr Leu Val Arg His Ala Tyr Lys Asn Pro Asn Glu Ile Tyr
610 615 620
tct gaa ata tct gaa gta gca aaa tta aag gat gct aag agt gaa gtt 1920
Ser Glu Ile Ser Glu Val Ala Lys Leu Lys Asp Ala Lys Ser Glu Val
625 630 635 640
aag aaa tca caa tat ttt agt acc ttt act ttg aga ggt agt tac aca 1968
Lys Lys Ser Gln Tyr Phe Ser Thr Phe Thr Leu Arg Gly Ser Tyr Thr
645 650 655
ggt gga gca tct aag ggg aaa tta gaa gat caa aaa gca atg aat aag 2016
Gly Gly Ala Ser Lys Gly Lys Leu Glu Asp Gln Lys Ala Met Asn Lys
660 665 670
ttt ata gat gat tca ctt aag aaa tta gat acg tat tct tgg agt ggg 2064
Phe Ile Asp Asp Ser Leu Lys Lys Leu Asp Thr Tyr Ser Trp Ser Gly
675 680 685
tat aaa act tta act gct tat ttc act aat tat aaa gtt gac tct tca 2112
Tyr Lys Thr Leu Thr Ala Tyr Phe Thr Asn Tyr Lys Val Asp Ser Ser
690 695 700
aat aga gtt act tat gat gta gta ttc cac gga tat tta cca aac gaa 2160
Asn Arg Val Thr Tyr Asp Val Val Phe His Gly Tyr Leu Pro Asn Glu
705 710 715 720
ggt gat tcc aaa aat tca tta cct tat ggc aag atc aat gga act tac 2208
Gly Asp Ser Lys Asn Ser Leu Pro Tyr Gly Lys Ile Asn Gly Thr Tyr
725 730 735
aag gga aca gag aaa gaa aaa atc aaa ttc tct agt gaa ggc tct ttc 2256
Lys Gly Thr Glu Lys Glu Lys Ile Lys Phe Ser Ser Glu Gly Ser Phe
740 745 750
gat cca gat ggt aaa ata gtt tct tat gaa tgg gat ttc gga gat ggt 2304
Asp Pro Asp Gly Lys Ile Val Ser Tyr Glu Trp Asp Phe Gly Asp Gly
755 760 765
aat aag agt aat gag gaa aat cca gag cat tca tat gac aag gta gga 2352
Asn Lys Ser Asn Glu Glu Asn Pro Glu His Ser Tyr Asp Lys Val Gly
770 775 780
act tat aca gtg aaa tta aaa gtt act gat gac aag gga gaa tct tca 2400
Thr Tyr Thr Val Lys Leu Lys Val Thr Asp Asp Lys Gly Glu Ser Ser
785 790 795 800
gta tct act act act gca gaa ata aag gat ctt tca gaa aat aaa ctt 2448
Val Ser Thr Thr Thr Ala Glu Ile Lys Asp Leu Ser Glu Asn Lys Leu
805 810 815
cca gtt ata tat atg cat gta cct aaa tcc gga gcc tta aat caa aaa 2496
Pro Val Ile Tyr Met His Val Pro Lys Ser Gly Ala Leu Asn Gln Lys
820 825 830
gtt gtt ttc tat gga aaa gga aca tat gac cca gat gga tct atc gca 2544
Val Val Phe Tyr Gly Lys Gly Thr Tyr Asp Pro Asp Gly Ser Ile Ala
835 840 845
gga tat caa tgg gac ttt ggt gat gga agt gat ttt agc agt gaa caa 2592
Gly Tyr Gln Trp Asp Phe Gly Asp Gly Ser Asp Phe Ser Ser Glu Gln
850 855 860
aac cca agc cat gta tat act aaa aaa ggt gaa tat act gta aca tta 2640
Asn Pro Ser His Val Tyr Thr Lys Lys Gly Glu Tyr Thr Val Thr Leu
865 870 875 880
aga gta atg gat agt agt gga caa atg agt gaa aaa act atg aag att 2688
Arg Val Met Asp Ser Ser Gly Gln Met Ser Glu Lys Thr Met Lys Ile
885 890 895
aag att aca gat ccg gta tat cca ata ggc act gaa aaa gaa cca aat 2736
Lys Ile Thr Asp Pro Val Tyr Pro Ile Gly Thr Glu Lys Glu Pro Asn
900 905 910
aac agt aaa gaa act gca agt ggt cca ata gta cca ggt ata cct gtt 2784
Asn Ser Lys Glu Thr Ala Ser Gly Pro Ile Val Pro Gly Ile Pro Val
915 920 925
agt gga acc ata gaa aat aca agt gat caa gat tat ttc tat ttt gat 2832
Ser Gly Thr Ile Glu Asn Thr Ser Asp Gln Asp Tyr Phe Tyr Phe Asp
930 935 940
gtt ata aca cca gga gaa gta aaa ata gat ata aat aaa tta ggg tac 2880
Val Ile Thr Pro Gly Glu Val Lys Ile Asp Ile Asn Lys Leu Gly Tyr
945 950 955 960
gga gga gct act tgg gta gta tat gat gaa aat aat aat gca gta tct 2928
Gly Gly Ala Thr Trp Val Val Tyr Asp Glu Asn Asn Asn Ala Val Ser
965 970 975
tat gcc act gat gat ggg caa aat tta agt gga aag ttt aag gca gat 2976
Tyr Ala Thr Asp Asp Gly Gln Asn Leu Ser Gly Lys Phe Lys Ala Asp
980 985 990
aaa cca ggt aga tat tac atc cat ctt tac atg ttt aat ggt agt tat 3024
Lys Pro Gly Arg Tyr Tyr Ile His Leu Tyr Met Phe Asn Gly Ser Tyr
995 1000 1005
atg cca tat aga att aat ata gaa ggt tca gta tct aga aag ctt 3069
Met Pro Tyr Arg Ile Asn Ile Glu Gly Ser Val Ser Arg Lys Leu
1010 1015 1020
gcg gcc gca ctc gag cac cac cac cac cac cac tga 3105
Ala Ala Ala Leu Glu His His His His His His
1025 1030
<210> 9
<211> 25
<212> DNA
<213> Artificial
<220>
<223> A primer for PCR (colG-F)
<400> 9
atgaaaaaaa atattttaaa gattc 25
<210> 10
<211> 27
<212> DNA
<213> Artificial
<220>
<223> A primer for PCR (colG-R)
<400> 10
ccggatccta tctagatacc cttaact 27
<210> 11
<211> 28
<212> DNA
<213> Artificial
<220>
<223> A primer for PCR (His-F)
<400> 11
gctctagaaa gcttgcggcc gcactcga 28
<210> 12
<211> 24
<212> DNA
<213> Artificial
<220>
<223> A primer for PCR (His-R)
<400> 12
cgggatccgg atatagttcc tcct 24
<210> 13
<211> 28
<212> DNA
<213> Artificial
<220>
<223> A primer for PCR (lac-F)
<400> 13
ccggcaagct tgcccaatac gcaaaccg 28
<210> 14
<211> 18
<212> DNA
<213> Artificial
<220>
<223> A primer for PCR (lac-R)
<400> 14
agctgtttcc tgtgtgaa 18
<210> 15
<211> 20
<212> DNA
<213> Artificial
<220>
<223> A primer for PCR (colH-F)
<400> 15
atgaaaagga aatgtttatc 20
<210> 16
<211> 27
<212> DNA
<213> Artificial
<220>
<223> A primer for PCR (colH-R)
<400> 16
ccggatccta tctagatact gaacctt 27
Claims (29)
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 삭제
- 하기 (i) 내지 (viii)에서 선택되는 콜라게나제의 카르복실 말단에 직접 또는 간접적으로 친화성 태그가 결합된 융합 콜라게나제를 코드하는 DNA, 또는 상기 DNA를 포함하여 이루어지는 발현 벡터에 의해 형질전환된 대장균을 배양해서 얻어지는 배양물을, 친화성 태그에 대응한 친화성 크로마토그래피로 정제함으로써, 콜라겐 결합 부위를 가진 융합 콜라게나제를 선택적으로 채취하는 것을 특징으로 하는 융합 콜라게나제의 제조방법:
(i) 서열번호:1 또는 2에 기재된 -110번에서 1008번까지의 아미노산 서열의 전부로 이루어진 콜라게나제;
(ii) 서열번호:1 또는 2에 기재된 -110번에서 1008번까지의 아미노산 서열에서 1~50개의 아미노산이 결실, 치환, 삽입 또는 부가된 아미노산 서열로 이루어진 콜라게나제;
(iii) 서열번호:1 또는 2에 기재된 -110번에서 1008번까지의 아미노산 서열과 80% 이상의 상동성을 가진 아미노산 서열로 이루어진 콜라게나제;
(iv) (i)에서부터 (iii)의 내에서 어느 하나에 기재된 콜라게나제로부터 서열번호:1 또는 2에 기재된 -1번에서 -110번까지의 아미노산 서열의 전부가 제거된 콜라게나제;
(v) 서열번호:5 또는 6에 기재된 -40번에서 981번까지의 아미노산 서열의 전부를 포함하는 콜라게나제;
(vi) 서열번호:5 또는 6에 기재된 -40번에서 981번까지의 아미노산 서열에서 1~50개의 아미노산이 결실, 치환, 삽입 또는 부가된 아미노산 서열을 포함하는 콜라게나제;
(vii) 서열번호:5 또는 6에 기재된 -40번에서 981번까지의 아미노산 서열과 80% 이상의 상동성을 가진 아미노산 서열을 포함하는 콜라게나제;
(viii) (v)에서부터 (vii)의 내에서 어느 하나에 기재된 콜라게나제에서 서열번호:5 또는 6에 기재된 -1번에서 -40번까지의 아미노산 서열의 전부가 제거된 콜라게나제. - 삭제
- 삭제
- 제17항에 있어서, 친화성 태그가 2개 이상 연속하는 히스티딘 잔기인 것인 제조방법.
- 제17항에 있어서, 콜라게나제가 클로스트리디움·히스트리티캄에 유래하는 것인 제조방법.
- 삭제
- 제17항에 있어서, 융합 콜라게나제가 서열번호:3에 기재된 -110번에서 1021번까지의 아미노산 서열의 전부로 이루어진 것인 제조방법.
- 제23항에 있어서, 융합 콜라게나제가 서열번호:3에 기재된 -1번에서 -110번까지의 아미노산 서열의 전부가 제거된 것인 제조방법.
- 삭제
- 제17항에 있어서, 융합 콜라게나제가 서열번호:7에 기재된 -40번에서 994번까지의 아미노산 서열의 전부로 이루어진 것인 제조방법.
- 제26항에 있어서, 융합 콜라게나제가 서열번호:7에 기재된 -1로부터 -40번까지의 아미노산 서열의 전부가 제거된 아미노산 서열로 이루어진 것인 제조방법.
- 제17항에 있어서, 융합 콜라게나제를 코드하는 DNA가 서열번호:4에 기재된 1번에서 3396번까지의 염기서열로 이루어진 DNA인 것인 제조방법.
- 제17항에 있어서, 융합 콜라게나제를 코드하는 DNA가 서열번호:8에 기재된 1번에서 3105번까지의 염기서열로 이루어진 DNA인 것인 제조방법.
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CA3112772A1 (en) * | 2013-02-01 | 2014-08-07 | Tohoku University | Method for separating liver cells from liver tissue |
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US11473074B2 (en) | 2017-03-28 | 2022-10-18 | Endo Global Aesthetics Limited | Method of producing collagenase |
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Biomol NMR Assign., Vol. 2, No. 2, pp. 127-129 (Epub 2008.07.22.) |
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CA2744286A1 (en) | 2010-05-27 |
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CN102216454B (zh) | 2013-05-29 |
NZ593239A (en) | 2013-01-25 |
DK2363461T3 (en) | 2015-03-02 |
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