KR0183980B1 - 이중특이성 및 올리고특이성 일가 및 올리고가 수용체 및 이를 포함하는 약제학적 조성물 - Google Patents

이중특이성 및 올리고특이성 일가 및 올리고가 수용체 및 이를 포함하는 약제학적 조성물 Download PDF

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KR0183980B1
KR0183980B1 KR1019900009252A KR900009252A KR0183980B1 KR 0183980 B1 KR0183980 B1 KR 0183980B1 KR 1019900009252 A KR1019900009252 A KR 1019900009252A KR 900009252 A KR900009252 A KR 900009252A KR 0183980 B1 KR0183980 B1 KR 0183980B1
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antibody
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edta
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amino acid
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보스레트 클라우스
헤르멘틴 페터
제만 게르하르트
쿨만 루드비크
스타인스트래써 악셀
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스타인 부크
베링베르케 아크티엔게젤샤프트
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    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
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    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
    • C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
    • C07K16/3007—Carcino-embryonic Antigens
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Abstract

내용 없음.

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이중특이성 및 올리고특이성 일가 및 올리고가 수용체 및 이를 포함하는 약제학적 조성물
제1도는 VHaCH1a-폴리펩타이드 스페이서-VHbCH1b를 도시한 것이다.
제2도는 중쇄 및 경쇄의 정확한 쌍을 갖는 하이브리드 분자를 도시한 것이다.
제3도는 VHaCH1a-폴리펩타이드 스페이서-VHbCH1b-폴리펩타이드 스페이서-VHaCH1a를 도시한 것이다.
제4도는 MAba의 2개의 F(ab) 단편과 MAb b의 1개의 F(ab) 단면을 함유하는 융합분자를 도시한 것이다.
제5도는 플라스미드 IgG3C F(ab')21H의 지도이다.
제6도는 플라스미드 M의 지도이다.
제7도는 플라스미드 VHa/VHbPcR 지도이다.
제8도는 플라스미드 pEVHa C의 지도이다.
제9도는 플라스미드 L의 작제도이다.
제10도는 플라스미드 X의 작제도이다.
제11도는 플라스미드 Z의 작제도이다.
제12도는 플라스미드 Y의 작제도이다.
제13도는 플라스미드 PEVT의 작제도이다.
제14도는 플라스미드 D의 지도이다.
제15도는 플라스미드 E의 지도이다.
제16도는 플라스미드 F의 작제도이다.
제17도는 플라스미드 G의 작제도이다.
제18도는 플라스미드 G1의 작제도이다.
제19도는 플라스미드 H의 작제도이다.
제20도는 플라스미드 I의 작제도이다.
제21도는 플라스미드 K의 작제도이다.
본 발명의 특이성이 2개 이상 상이한 항체 F(ab) 단편을 암호화하는 DNA를 적합한 링커를 사용하여 융합시키는 유전자 조작에 의해 제조된 이중특이성 및 올리고특이성 일가 및 올리고가 수용체에 관한 것이다. 이와 관련하여, 하나의 특이성은 바람직하게는 세포막상에 또는 간질내에 위치하는 종양-연관된 항원(TAA)의 에피토프에 지시되거나, 종양 내피(TE)내의 에피토프에 대해 지시되는 반면에, 다른 특이성은 고분자량 또는 저분자량의 리간드에 관한 것으로, 예를 들면, 킬레이트제인 에틸렌디아민테트라아세테이트 및 디에틸렌트리아민펜타아세테이트로써 Y90 복합형태(각각 EDTA-Y90 및 DTPA-Y90)로 반응한다. 특히 바람직한 양태에서, 킬레이트제와의 결합은 fos-jun 상호작용(또는 아비딘-바이오틴 상호작용)을 경유하여 킬레이트 수용체 암(arm)상에서 일어난다. 다른 바람직한 특이성은 촉매 특성을 갖거나, 동일한 종양 세포상의 다른 TAA 또는 림프구 세포상의 수용체에 결합하는 것이다.
이중특이성 항체는 지금까지 하기의 방법에 의해 제조되어 왔다 :
1. 헤테로 이중작용성 링커를 경유하여 특이성이 다양한 항체의 화학적인 커플링[H. Paulus, Behring Inst. Mitt. 78, (1985), 118-132]
2. 기존에 사용되어온 하이브리드와 알려지지 않은 다양한 모노클로날 항체(MAb)와의 융합, 및 이중특이성 일가 부위의 분리[참조 : U.S. Staerz and M.J. Bevan, Proc. Natl. Acad. Sci. USA 83, (1986) 1453-1457]
3. 쥐의 골수종 세포 또는 다른 진핵성 발현 시스템내로 2개의 상이한 MAb의 경쇄 및 중쇄 유전자(4개의 유전자)의 형질감염 및 이중특이성 일가 부위의 분리[참조 : U. Zimmermann, Rev. Physio. Biochem. Pharmacol. 105(1986), 176-260; J. Van Dijk et al., Int. J. Cancer 43, (1989), 334-349].
이러한 유형의 이중특이성 항체는 악성종양을 치료하거나 진단하는데 사용한다. 이 과정의 원리는 제1단계에서는 장시간에 걸쳐 높은 용량으로 이중특이성 거대분자를 주입하여 2개의 특이성중 하나에 의해 표적세포상에서 인지되는 에피토프를 포화시킴을 포함한다.
제2단계에서는 수일 동안 치료를 중단하고, 비-표적 조직으로부터 비-특이적으로 흡착된 이중특이성 항체를 자동 제거함을 포함한다. 이러한 자동제거는 당잔기(바람직하게는 갈락토즈)와 결합하고, 이중특이성 수용체의 항-종양 암에 대해 지시되는 항-유전형 항체를 주입함으로써 가속시킬 수 있다.
제3단계에서는 세포내에 축적되지 않고, 체내에서 짧은 체류 시간을 가지며,90Y,186Re,188Re,189Re,99mTc 또는111In과 같은 베타-및 감마-방사제에 대해 높은 복합상수를 갖고, 이중특이성 수용체의 제2특이성에 고친화성으로 결합하는 방사성 표지된 친수성의 저분자량 리간드의 정맥내 주사를 포함한다. 이 단계에서는, 표적 조직상에 연장된 체류와 관련하여, 방사활성 리간드가 농축됨으로써 그결과 표적 조직을 선택적으로 파괴시키고 예를 들어 전이의 진단을 가능케 한다.
본 발명에 이르러, 본 발명은 요구상태에 따라, 특정 에피토프에 대한 일가 또는 올리고가 결합 부위를 가지며 적합한 링커를 사용한 유전자 조작에 따라 생성된 이중 특이성 및 올리고 특이성 수용체를 제공한다. 이는, MAb b의 VH영역의 N-말단이 Mab a의 CH1 영역의 C-말단에 폴리펩타이드 스페이서를 경유하여 공유결합하는 방식으로, 항체 a 및 b의 VH및 CH1부분을 암호화하는 유전자 단편을 표 1에 예시적으로 도시된 적합한 합성 올리고뉴클레오타이드를 이용하여 연결시키는 것을 포함한다(제1도). VHaCH1a-폴리펩타이드 스페이서-VHbCH1b 유전자 작제물을 항체 a 및 b의 경쇄를 암호화한 유전자와 함께 진핵세포(예, 마우스의 골수종 세포)내로 형질 감염시킨다. CH1a, CH1b, CKa 및 CKb 영역은 고정 영역의 접촉 부위에서 상반된 전하가 만나거나 (CH1a(+)CKa(-); (CH1b(-)CKb(+))(+=양성, -=음성), 상반되는 접촉부위가 각 경우에 소수성이거나 각 경우에 친수성이 되는 방식으로 변형된다. 이는 형질 감염 종양 세포(transfectoma)가 중쇄와 경쇄의 정확한 쌍을 갖는 하이브리드 분자(제2도)를 선별적으로 발현함을 의미한다.
여기서, 항체 a는 항종양 항체의 대표적인 예이며, 항체 b는 저분자량 리간드, 바람직하게는 킬레이트제 DTPA-Y90 또는 EDTA-Y90에 대한 항체를 나타낸다.
따라서, 이중특이성- 또는 올리고특이성 수용체는, 상응하는 경쇄와 관련하여 필요한 이동성이 존재하고 항원 결합이 장애를 받지 않도록, 적합한 링커를 경유하여 특이성이 다양한 항체의 VH와 Ch1 영역을 유전공학적으로 연결시킨 작제물이다.
항원-결합 부위를 결합가 또는 결합부위라고 한다. 그러므로, 2개의 특이성이 존재할 때 이중특이성 일가 수용체는 각 경우에 하나의 항원-결합 부위를 갖는다. 결국, 이중특이성 3가 수용체는 하나의 특이성에 대해 1개의 항원-결합 부위를 갖고 다른 특이성에 대해 2개의 항원-결합 부위를 갖는다. 종양 항원(MAb a)에 대해 이가이고 EDTA-Y90(MAb b)에 대해 일가인 이중특이성 수용체는 사술한 올리고 뉴클레오타이드 링커를 이용하여, 상기의 중쇄 유전자 작제물을 Mab a의 VH및 CH1 영역을 암호화하는 유전자 부분(제3도)에 연결시킴으로서 MAb b의 CH1 영역의 C 말단이 폴리펩타이드 스페이서에 의해 MAb a의 VH영역의 N-말단에 연결되도록 하여 제조한다. 이들 유전자 작제물을 MAb a 및 b에 속하는 경쇄의 유전자와 함께 진핵세포(예, 골수종 세포)내에 형질감염시킨다. 상술한 바와 같이, 각각의 경우에 소수성 또는 친수성인 상보 전하 또는 접촉 부위를 갖는 CH1 및 CK영역이 제공된다. 형질감염종양 세포는 MAb a의 2개의 F(ab) 단편 및 MAb b의 1개의 F(ab) 단편을 함유하는 융합 분자를 발현한다. 펩타이드 링커의 이동성은 종양 세포에 대한 MAb a의 2개의 F(ab) 암의 배열과 동시에, 세포간 스페이스에 대한 MAb b의 F(ab) 암의 배열을 가능케 한다. 상응하게 특이성이 동일하거나 상이한 결합 부위를 추가로 가하는 것이 가능하다. 또한, 작제물내에 특이성의 서열을 자유로이 결합시키는 것도 가능하다.
결국, 본 발명은 세포막상에 또는 간질내에 위치하는 에피토프(예, TAA 또는 TE)에 대한 특이성 및 세포외 공간내에 편재해 있는 저분자량 또는 고분자량 리간드에 대한 특이성을 모두 갖는 이중특이성 또는 올리고특이성, 일가-또는 올리고가수용체에 관한 것이다. 이와 관련하여, 1개의 특이성은, 독일연방공화국 특허원 제 P 39 09 799.4 호에 제시된 바와 같이, 종양-특이성 항체에 의해 형성되는 것이 바람직한 반면, 다른 특이성은 DTPA-Y90 또는 EDTA-Y90에 대해 지시하는 것이 바람직하다. 특히 바람직한 양태에서, 결합은 fos-jun 상호 작용을 경유하여 킬레이트 수용체 암 상에서 킬레이트제와 함께 이루어진다(실시예 5 참조). 본 발명의 다른 바람직한 변형은 촉매 활성이 있는 특이성의 혼입을 포함한다. 게다가, 2개의 특이성을 갖는 3가에 대하여 예시적으로 제4도 제시한 바와 같이, 특이성의 서열 또는 결합가에 대한 선택에 있어서는 제한이 없다.
본 발명에 따른 특히 바람직한 작제물은 표 2, 3, 4 및/또는 5의 V 유전자를 함유하는 것이다. 이들 서열 및 특성을 갖는 항체는 독일연방공화국 특허원 제 P 39 09 799.4호에 기술되어 있다. 게다가, 상보성 결정 영역(CDR)은 가바트(Kabat) 및 부(Wu)의 방법[참조; Sequences of Proteins of Immunological Interest, US Dept. of Health and Human Services, US Government Printing Office(1987)에 의해 동정될 수 있다. 상기의 모노클로날 항체에 의해 정의된 에피토프에 대한 특이성을 함유하는 작제물도 역시 바람직하다.
추가로, 본 발명은 상술한 작제물의 유전공학적 제조방법, 및 표적세포의 억제 및 진단용 약제를 제조하는데 있어 상기 작제물의 용도에 관한 것이다. 이것은 제1단계에서, 작제물을 주입한 후 표적세포상에서 관련된 에피토프를 포화시키고, 일정시간 후, 비특이적으로 흡착된 또는 결합되지 않은 작제물을 제거함을 포함한다. 이의 다음 단계는 세포내에 축적되지 않고 본질적으로 세포독성이거나 경우에 따라 다른 단계로서 체외 영향에 의해 세포독성으로 활성화되는 저분자량 또는 고분자량 리간드의 주입 및 연속적인 특이적 결합을 포함한다. 상기 유형의 과정의 예로 효소적 활성화, 프로드럭의 극초단파 조사에 의한 활성화 또는 레이저 광선에 의한 활성화를 들 수 있다.
또한, 본 발명을 실시예 및 특허청구의 범위에서 더 기술한다.
[실시예 1]
항-DTPA-Y90 또는 EDTA-Y90 MAb의 제조
이소티오시아나토벤질-DTPA(일반식 2)를 합텐으로서 문헌[참조 : N.W. Brechbiel et al., Inorganic Chemistry 25, (1986)2772-2781]에 기술된 방법에 따라 HSA 분자당 19개의 벤질-DTPA 분자가 유도체화되는 수준으로 사람 혈청 알부민(담체로서의 HSA)상에 공유결합시킨다. 냉 Y가 복합화된 합텐-담체 복합체 20㎍을 0일째에 프로인드 보조제, 7일 및 14일째에 불완전 프로인드 보조제 및 21일째에 PBS와 함께 Balb/c 마우스내로 피하 주사한다. 24일째에, 최고의 항-DTPA 항체 역가를 갖는 마우스의 비장을 SP2/0-Ag14 골수종 세포주와 융합시킨다[참조; Shulman et al., Nature 276, (1978) 269]. 생성된 하이브리도마를 DTPA-특이적 ELISA로서 DTPA 및 EDTA에 대한 고-친화성 MAb의 생성 여부를 시험한다. ELISA는 HSA-벤질-DTPA-Y가 함유된 용액이 적재된 고체상을 포함한다. 시험될 MAb를 함유하는 상층액을 유리된 킬레이트 또는 이의 금속 이온 복합체와 함께 예비 항온 처리하고, 특이적 고체상에 대한 이들의 결합 여부를 측정한다. 이러한 목적을 위해 항-마우스 면역 글로불린 항체에 결합하는 효소 증폭 시스템을 사용한다. 이들 방법은 별첨 1a 및 1b에 상세히 기술되어 있다.
별첨 1e에 기술된 특성을 갖는 MAb는 상기 검정 시스템을 사용하여 수득하였다.
많은 다른 항-DTPA/EDTA MAb와는 대조적으로, 이들 MAb는 저온 보존된 조직상에서 APAAP 기술[참조 : Cordellet al., J. Histochem. Cytochem. 32:219, 1984]을 사용하여 발견되는 바와 같이, 정상적인 사람의 조직에 결합하지 않는다. 따라서, 이들 MAb는 진단 및 치료용으로 생체내에서 사용 가능하다.
사용된 경쟁자는 비-복합 형태 및 복합 형태의 킬레이트 DTPA 및 EDTA이다(별첨 1c). 또한, 구조적으로 관련된 화합물 트란스아코니트산 및 1,2-디아미노에탄을 억제제로서 사용한다(별첨 1e). MAb BW2050/174가 생체내에서 사용하기에 특히 적합하며, 이는 모든 다른 MAb와는 대조적으로 EDTA-Y와 선별적으로 결합함을 보여준다[참조; 별첨 1e, EDTA-Y에 대해 저 과량 경쟁자(100x) 다른 EDTA 복합체에 대해 고과량]. 따라서, 하이브리드 2050/174는 안정하며 이중특이성 수용체내에서 EDTA-Y 암을 전개시키는데 사용된다.
[실시예 2]
VHlaCHl-링커-VHlbCHl 유전자 작제물의 제조 및 발현
본 원에서 사용된 기술은 달리 제시하지 않는 한, 하기의 방법을 이용한 것이다 : Molecular Cloning, A Laboratory Manual; Sambrook, Fritsch, Maniatis; Cold Spring Harbor Laboratory, 1982(pp. 11-44,51-127,133-134,141,146,150-167,170,188-193,197-199,248-255,270-294,310-328,364-401,437-506)and from Molecular Cloning, A Laboratory Manual,Second Edition; Sambroo k,Fritsh,Maniatis; Cold Spring Harbor Laboratory Press,1989,(pp. 16.2-16.22,16.30-16.40,16.54-16.55).
사람 IgG3C 유전자는 EMBL3 파아지내 사람 유전자 뱅크로부터 분리하였다 : [참조 A.M. Frischauf et al., J. Mol. Biol. 170, 827-842(1983) and G.H.A.Seemann et al., The EMBO Journal 5(1986), 547-552].
한편으로는 CHl 엑손 및 힌지 엑손(제5도)만을 함유하고, 다른 한편으로는 CHl 엑손 및 HLA B27 유전자의 3'NT 영역(제6도,플라스미드 M내의 단편 M)을 함유하는 작제물을 독일연방공화국 특허원 제 P 38 25 615.0호에 기술된 바와 같이 IgG3C 유전자로부터 제조한다.
VHa 및 VHb 유전자를 Orlandi 등에 의해 문헌[Proc. Natl. Acad Sci. USA 86,(1989),3833-3837]에 기술된 바와 같이 하이브리드 클론 a 및 b의 mRNA로부터 증폭시키고 M13 벡터내로 클로닝시킨다(VHa PCR 및 VHb PCR)(제7도). VHa 유전자를 HindIII-BamHI 단편으로서 진핵 세포 발현 벡터 pEVH내로 클로닝시킨다[Simon et al., Nucl. Acids. Res. 16. (1988), 354](제8도). 이 결과에 의해 수득된 것은 플라스미드 pEVHa C 이다.
CHl 및 하나의 힌지 엑손(제5도)과의 사람 IgG C 유전자 서브클론은 CHl 엑손과 힌지 엑손 사이에 PstI 분해 부위를 함유한다. VH유전자는 5' 말단에 PstI 분해 부위를 함유한다. 5' 말단에서 IgG C 유전자의 CHl+IH 서브단편상의 PstI 분해부위의 영역과 중복되고 3' 말단에서 VHb 유전자의 PstI 분해 부위와 중복되도록 링커 올리고뉴클레오타이드를 고안한다. 이 링커 올리고뉴클레오타이드를, PstI 분해 부위를 이용하여, pUC18 플라스미드의 PstI 절단부위 내로 클로닝시킨다(제9도). 이 결과 수득된 것은 플라스미드 클론 L이다.
CH+l 엑손과 힌지 엑손을 갖는 IgG3C 유전자 서브 단편을 함유한 플라스미드를 PstI 및 BamHI으로 분해하고 VHb PCR로부터 PstI-BamHI 단편으로서 분해된 VHb 유전자 단편에 연결시킨다(제10도). 이 결과 수득된 것은 플라스미드 X이다.
플라스미드 X를 PstI으로 분해하고 플라스미드 L을 PstI으로 분해하여 얻은 링커 단편에 연결시킨다(제11도). 핵산 서열 분석 방법을 사용하여 링커가 CHl과 VHb 사이에 올바른 배향으로서 인트론 3과 링커 엑손 사이의 인트론/엑손 연결을 방해하지 않고 링커아 VHb 유전자 사이의 연결부에서 판독 프레임을 방해하지 않도록 클로닝된 크론 Z를 동정한다.
플라스미드 pEVaC를 BamHI으로 분해하고 BamHI으로 플라스미드 M을 절단하여 얻은 단편 M에 연결시킨다. 제한 분석법을 사용하여 단편 M을 정확한 배향으로 함유하는 클론 Y를 동정한다(제12도).
플라스미드 Y를 BamHI으로 부분 분해하고 플라스미드 X를 HindIII 및 BamHI으로 분해하여 얻은 단편(CHl-링커-VHb)에 연결시키면, 결국 말단부가 충진된다. 뉴클레오타이드 서열분석법 및 제한 지도 작성법을 사용하여 모든 엑손의 정확한 배향과 함께 융합 유전자 VHa CHl-링커-VHb CHl을 함유하는 플라스미드 클론 PEVT를 동정한다(제13도).
항체 a F(ab) 항체 b F(ab) 융합 단백질을 발현시키기 위하여, 플라스미드 PEVT를 항체 a와 b의 경쇄 암호화 유전자가 함유된 플라스미드와 함께 적합한 진핵발현 세포내로 형질 감연시킨다.
[실시예 3]
2개의 상이한 MAb(4개의 유전자)의 경쇄 및 중쇄 유전자의 형질감염
면역글로불린 유전자의 분리는 독일연방공화국 특허원 제 P 39 09 799.4호에 기술되어 있다.
벡터내로 클론된 유전자는 벡터를 X63Ag 8.653 골수종 세포로 선형화한 다음 전기영동에 의해 형질감염시킨다(참조 : H. Stopper et al., Biochem. Biophys. Acta 900(1987), 38-44). 선택배지에서 성장시킨 형질감염 종양세포를 특이적 RIA 중에서 이중특이성 일가 MAb의 생산에 대해 시험한다. 이 RlA는 고형상에 흡착된 TAA를 포함하며, 카제인에 의해 비-특이적 부위를 폐쇄시킨 후, 이위에는 분석될 형질감염종양세포 상층액이 위치하게 된다.90Y 또는99mTC와 복합화시킨 DTPA 또는 EDTA를 가하고 과량을 세척해낸 후, 고체상에서 증강된 방사성 시그날에 의해 이중특이성 일가 항-TAA x 항-EDTA MAb를 분비하는 형질감염 종양 세포를 검출하는 것이 가능하다.
형질감염종양세포 9는 한정된 희석 클로닝으로 안정화시키고 세포 배양으로 증가시킨다. 세포 배양물 상층액을 10배 농축시키고, 단백질 A 크로마토그래피로 MAb 분획을 정제하며(참조 : P.L. Ey et al., Immunochemistry 15, (1978), 429), 이중특이성 일가 MAb를 함유한 분획을 음이온 교환 크로마토그래피로 정제한다[참조 : J. Van Dijk et al., Int. J. Cancer 43, (1989), 344-349].
[실시예 4]
생물학적 효능
이중특이성 일가 MAb를 함유한 정제된 단백질(BW 431/26xBW 2050/174)을 사람 종양 이종이식물(CoCa 4)을 지니고 있는 누드 마우스에 0, 3, 5, 8, 10 및 12일째에 500㎍의 용량을 정맥내 주입한다. EDTA-Y90 50μCi를 27 내지 30일째에 각 동물에 정맥내 주입한다. 두번째 그룹의 동물들에게 같은날에 이중특이성 MAb 대신에 500㎍의 MAb BW 431/26, 및 EDTA-Y90 주입물을 상기 기술한 바와 같이 주입한다.
종양이 있는 제3그룹에게는 MAb 및 EDTA-Y90 대신에 PBS(종양-성장 대조군으로서)를 주입한다. 종양성장은 6주간 지속됐다. EDTA-Y90의 주입으로 이중특이성 일가 MAb가 주입된 그룹에서 종양성장이 현저하게 억제된 반면, MAb BW 431/26을 주입하고 EDTA-Y90으로 처리된 동물에서는 단지 PBS만을 주입한 동물에 비해 종양성장의 억제가 나타나지 않았다.
이런 데이타들은, 독소원으로서 EDTA-Y90과 협력하여 이중특이성 일가 MAb의 선택적 종양-치료 효능을 나타내고 있다.
더욱 바람직한 종양-치료 효과는 올리고가/이중특이성 또는 올리고특이성 수용체에 의해 수득되는데, 이는 TAA에 이가 결합을 하기 때문에 종양에 이들이 오래남아 있을 수 있음으로 리간드가 종양 위에 좀더 오래 높은 농도로 남아 있기 때문이다.
일반적으로 이와 같은 종양의 치료 및 진단에 있어 부작용을 일으키지 않고 안전하게 사용될 수 있는 항체의 용량은 각각 0.01 내지 30㎎/㎏(체중) 및 0.001 내지 0.1㎎/㎏(체중)의 범위내임이 당해 분야에 공지되어 있다.
[실시예 5]
항-킬레이트 암의 결합성 증가에 의한 이중 또는 올리고특이성 거대분자의 생물학적 효능의 최적화
올리고특이성 거대분자의 항-킬레이트 암에 대해 세포외적으로 분포되는 친수성 킬레이트의 효율적인 부착에 영향을 끼치는 절대적인 인자는 이 암의 킬레이트에 대한 결합성이다. 모노클로날 항체의 상응하는 에피토프에 대한 친화도는 105내지 10111/ml의 범위이다. 이들 결합 강도가 효율적인 방사 면역치료요법에 필요한 킬레이트의 양을 종양상에 위치시키기에 불충분하기 때문에, 하기 실시예에서 fos-루이신-지퍼 펩타이드(fos-펩타이드)와 jun-루이신-지퍼 펩타이드(jun-펩타이드)[참조 : Erin K. O'Shera et al., 245, 1989]간의 극도로 강한 상호작용이 항-킬레이트 암상에 킬레이트를 가능한한 견고히 고정시키기 위해 사용됐다. 이런 강한 fos-jun 상호 작용을 이용할 수 있도록 하기 위해, 바람직하게는 fos 펩타이드를 킬레이트(DTPA)에 공유결합시키는 것이 필요하다. 이 목적을 위해 제1단계에서 이소티오시아네이토벤질-DTPA를 히드라진(또는 디아미노알칸)과 반응시키는 것도 가능하다. 제2단계에서는, 상기 방법에서 생성된 DTPA-벤질티오카브아지드를 N-(γ-말레이미도부티릴옥시)석신이미드 또는 동족체와 반응시켜 DTPA-벤질(γ-말레이미도부티릴)티오카브아지드를 수득할 수 있다. 제3단계에서는, 상기 화합물을 아미노-말단 시스테인의 유리 SH-그룹을 통해 글리신-글리신-시스테인(제1도)에 의해 연장된 fos-펩타이드에 연결시킨다. 제4단계에서는, 상기 방법으로 생성된 fos-펩타이드-DTPA 접합체를 염화 이트륨으로 착화시킨다. 상기 방법에서 생성된 fos-펩타이드-DTPA-Y 접합체 착물은 생체내에서 이중-또는 올리고특이성 거대분자의 jun-펩타이드 암상에 첨가하기 위해 사용할 수 있다. 상기 실시예의 합성은 하기에 상세히 설명한다.
A) fos-EDTA-Y 접합체 착물의 제조
단계 1 :
EDTA-벤질티오카브아지드의 합성
이소티오시아네이토벤질-EDTA(SCN-Bm-EDTA)(30mg,54μmol)을 10%(v/v) 수성 하이드라진내에서 1시간 동안 교반시킨다. 고 진공하에서 용매를 제거한 후, 잔사를 고 진공하 오산화인 위에서 건조시키고 최종적으로 동결 건조시킨다. 생성물을 DOWEX WX 2(H+형태)로 중화시키고 다시 동결 건조시킨다(28mg 수득).
단계 2 :
EDTA-벤질(γ-말레이미도부티릴)티오카브아지드의 합성
제1단계에서 제조한 EDTA-벤질티오카브아지드(20mg : 34μmol) 및 N-(γ-말레이미도부티릴옥시)석신이미드(8mg,29μmol=0.9당량)를 무수 디메틸포름아미드중에서 1시간 동안 교반한다. 혼합물을 증발 건조시킨 후, 잔사를 고진공하에 건조시킨다.
단계 3 :
fos-펩타이드중의 아미노-말단 시스테인에 대한 EDTA-벤질(γ-말레이미도부티릴)티오카브아지드의 커플링
인산염-완충 염수(2ml)중 fos-펩타이드(4.8mg,1μmol)의 용액(단계 3.1 참조)을 디메틸포름아미드(400㎕)중 단계 2에서 수득한 생성물 혼합물의 현택액(4mg)과 혼합한 후, 실온에서 1시간 동안 배양한다. 반응 혼합물을 인산염-완충 염수중 Sephadex G15 컬럼상에서 겔 여과시킨다. 단백질-함유 용출액을 수집하여 -30℃에 보존한다(4.2mg 수득).
단계 3.1
N-말단 GGC가 연장된 fos-펩타이드(1 1)의 아미노산 서열
Ac-CGGyLTDTLQAETDQLEDKKSALQTEIANLLKEKEKLEFILAAYy 문자는 하기의 아미노산을 나타낸다 : A=알라닌, C=시스테인, D=아스파르트산, E=글루탐산, G=글리신, I=이소루이신, K=라이신, L=루이신, M=메티오닌, N=아스파라긴, Q=글루타민, R=아르기닌, S=세린, T=트레오닌, V=발린, Y=티로신.
메리필드 고상법(Merrifield solid-phase method)(참조 : Stewart and Young. Solid Phase Synthesis, Pierce Chemical Company, 2nd edition, Rockford Ill.)에 따라 자동 펩타이드 합성기(Applied Biosystems Model 430A)를 사용하여 3급-부틸옥시카보닐 보호그룹을 지닌 올리고펩타이드를 합성한다. 페닐아세트아미도메틸-폴리스티렌 지지체로 올리고펩타이드를 분해한다. 보호그룹을 제거한 후(참조 : Tom et al., 1983, J. Am. Chem. Soc 105, 6442-6455), 문헌(참조 : Rivier 등의 J. Chromatography 288, 303-328, 1984)에 기술된 바와 같이, 역상 크로마토그래피(PepRPC 컬럼, Pharmacia)로써 올리고펩타이드를 정제한다.
단계 4 :
단계 3에서 제조한 fos-펩타이드-EDTA 접합체를 사용한 fos 펩타이드-EDTA-이트륨 킬레이트의 제조
단계 3에서와 같이 제조한 fos-펩타이드-EDTA 접합체(4.2mg)을 배출 한계가 분자량 1000인 투석 튜브(Spectrum 제조원)에서 등장염수/0.1M 시트르산나트륨(pH 7.0)에 대해 투석시킨 후, 등장염수/0.1M 시트르산 나트륨(pH 7.0) 3ml에 용해시킨 염화 이트륨 6mg과 혼합한다. 1시간 후, 인산염-완충 염수에 대한 역-투석을 수행하고, 킬레이트 용액을 -30℃에서 보관한다. 상기 실시예에 기술된 fos-펩타이드-EDTA-이트륨 킬레이트를 리간드로 사용하여 이중 또는 올리고특이성 거대분자의 jun-펩타이드 암에 강력하게 결합시킨다. 상기 상호 작용에 특히 적합한 이중특이적 거대분자의 작제는 하기 실시예에 기술되어 있다.
B) MAb-jun 융합 분자의 작제
특별한 언급이 없는 한, 문헌[Maniatis et al.(Laboratory Manual EMBL(1982), Heidelberg), and Sambrook(Mlecular Cloning : A Laboratory Manual]에서 사용된 기술을 사용한다.
단계 1 :
사람 IgG3 C 유전자를 EMBL3 파아지중 사람 유전자 은행으로 부터 분리한다(참조 : A.M. Frischauf et al., J. Mol. Biol. 170, 827-842, 1983 and G.H.A. Seemann et al., The EMBO Journal 5, 547-552, 1986). IgG3 C 유전자(제14도)의 CHl 엑손과 제1힌지 엑손만을 함유하는 작제물(D)은 독일연방공화국 특허원 제 P 38 25 615.0 호에 기술된 IgG3 C 유전자로부터 제조한다.
사람 HLA B27K 유전자는 독일연방공화국 특허원 제 P 38 25 615.0 호에 기술된 바와 같이 동일한 유전자 은행으로부터 분리한다. HLA B27K 유전자(제15도)의 C3 엑손과 3'NT 영역만 함유하는 작제물(E)은 HLA B27K 유전자로부터 제조한다.
단계 2 :
플라스미드 E를 XbaI로 HLA B27K 유전자의 C1 엑손 및 3'NT 영역을 절단하고 단편을 분리한 후, 작제물 D의 XbaI 분해 부위내에 클로닝시킨다. 제한분석과 헥산 서열 분석을 사용하여 정확한 5'-3' 배향 3'내에 HLA B27K 유전자의 C3 엑손과 3'NT 영역을 함유하는 클론 F를 IGg3 C 유전자 단편으로부터 동정한다(제16도).
단계 3 :
엔도뉴클레아제 HindIII 및 EcoRI를 사용하여 클론 F의 삽입물을 플라스미드로부터 절단하고 Ml3mp 18 이-본쇄(DS) 파지의 HindIII 및 EcoRI 분해 부위 사이에 클로닝시킨다. 항체/HLA 융합 유전자 단편을 함유하는 파지 클론 G를 분리한다(제17도).
단계 4 :
문헌[참조 : T.A. Kunkel. 1985. Proc. Natl. Acad. Science, U.S.A., 82, 488-492]의 방법에 따라 파지 클론 G로부터 우라실 일본쇄를 제조한다. 일-본쇄 파지를 돌연변이 유발성 올리고뉴클레오타이드 1 및 2(표 6)로 하이브리드화시킨 후, 올리고뉴클레오타이드 사이의 갭을 클레나우 DNA 폴리머라제 및 T4 리가제로 채운다.이 콜라이내에 형질 전환시킨 후, 제한 분석 및 핵산의 서열 분석을 사용하여 힌지 엑손을 5'말단에서 SstI 제한 절단부위가 결실된 파지클론(G)을 동정한다. 동시에, SstI 및 SphI 제한 절단부위를 힌지 엑손의 3' 말단에 도입한다(제18도). SstI 절단부위를 결실시키기 위해, 힌지 엑손의 2번째 코돈의 세번째 염기를 C로부터 G로 전환시킨 후, SstI 및 SphI 분해 부위를 도입시키기 위해, 염기 5'GAGCTCGGGGCA3'를 힌지 엑손의 15번째 및 16번째 코돈 사이에 도입시킨다(표 7).
단계 5 :
파지 클론 G'의 이본쇄 DNA를 SphI로 완전히 및 SstI으로 부분적 분해한다. 합성 올리고뉴클레오타이드 Jun I 및 Jun II(표 8)를 혼합하여 각각의 말단에 절단된 SphI 및 SstI 제한 분해 부위를 함유하고 Jun 루이신 지퍼를 함유하는 펩타이드를 암호화하는 이본쇄 DNA 단편을 수득한다(참조 : O'Shea et al., Science. 245, 646-648, 1989).
이본쇄 DNA 단편을 F' 파지 클론의 SstI 및 SphI 제한 분해 부위내에 클로닝시킨 후, Jun 지퍼 펩타이드에 대한 서열이 힌지 엑손내에 삽입되어 있는 유전자 작제물을 함유한 파지 클론 H를 동정한다(제19도).
단계 6 :
이본쇄 파지 H의 삽입물을 제한 엔도뉴클레아제 HindIII 및 EcoRI로 절단하고, 말단을 T4 폴리머라제로 채운다음 SmaI-분해된 KsF 벡터내에 클로닝시킨다(참조 : Stratagene, 11099 North Torrey Pines Road, La Jolla California 92037). BamHI 분해 부위에 의해 양측이 플랭킹되어 있는 배향(제20도)으로 항체/Jun/HLA 융합 유전자를 함유하는 플라스미드 클론 I을 동정한다.
단계 7 :
KS 클론 I로부터의 항체/Jun/HLA 융합 유전자를 BamHI로 절단하고 특이적 작용성 면역글로불린 V 유전자를 함유하는 발현 플라스미드 pABStop(Behringwerke AG)내에 클로닝시킨다. 특이적 V 유전자는 상기 특허원 제 P 39 09 799.4 호에 기술된 바와 같이 수득한다. VH유전자의 하부에 항체/Jun/HLA 융합 유전자 작제물을 정확한 배향으로 함유하는 발현 플라스미드 K를 동정한다(제21도).
특이적 MAb의 경쇄에 대한 유전자를 함유하는 플라스미드를 플라스미드 K 및 내성 유전자를 지닌 플라스미드와 공형질전환(cotransformation)으로 인해, 힌지 영역내에 더이상의 호모이량체(Jun/Jun)가 형성되지 않도록 하는 방식으로, 변형되어 있는 2개의 Jun 지퍼 펩타이드를 함유하는 특이적 항체 f(ab')2단편이 발현된다.
[실시예 6]
종양에 있어 이중 또는 올리고특이성 수용체 양의 최적화 및 혈액 및 정상 조직내에서 이의 최소화
다른 연구자들에 의한 과학적 연구에 의하면, 50KDa를 초과하는 거대분자에 의한 고체 종양의 침투는 서서히 발생하며, 보통 종양내 가장자리 영역 또는 일부지역에 도달한다는 것이 밝혀졌다. 이 연구는 소량의 거대분자를 1회 주입함을 포함하는 시험을 기초로 한다. 이와는 반대로, 본 발명자들은 다량의 이중 또는 올리고 특이성 수용체를 반복적으로 정맥주입(10x250㎍ 수용체/마우스, 10일간)하여 누드 마우스 이종 이식내 완전한 종양 덩이를 실질적으로 침투시킬 수 있음을 발견하였다. 더우기, 이중- 또는 올리고특이성 수용체들은 TAA에 특이적으로 결합하기 때문에, 이들은 종양세포막상 및 종양 간질내에서 오랜기간(20일 이상) 동안 다량으로 부착되어 있다. 이 결과는 사람의 결장 및 췌장 종양 이종이식의 저온 저장된 얇은 단면에 있어서 간접적인 알칼리성 포스파타제 기술을 사용하여 수득하였다.
이 기간중(단지 10일 후) 이중- 또는 올리고특이성 수용체 분자는 분해 및 분비에 의해 TAA-음성 정상 조직 및 혈액으로부터 이미 제거되었다. 이러한 제거기간을 단축시키기 위해, 이중- 또는 올리고특이성 수용체를 10일간 주입한 후 24시간째에, 단지 결합되지 않은 이중 또는 올리고 특이성 수용체 분자의 항-TAA 암과만 반응하는 항-유전형 MAb(항 Id)를 정맥 주입(1 X 50㎍의 항 Id)한다. 이러한 일회의 주입에 의해 혈액으로부터 결합되지 않은 이중- 또는 올리고특이성 수용체 분자의 제거가 촉진되며 간 및 비장에서의 대사 속도가 향상된다.
상기 조작을 기본으로 하여, 이중- 또는 올리고특이성 수용체의 침투 및 결합 상태가 완결된 후 단지 4일째에 킬레이트(EDTA-Y90)를 주입할 수 있다. 하기의 치료 섭생(누드 마우스의 경우)는 이 연구에 의해 얻은 것이다.
a) 매회 이중- 또는 올리고특이성 수용체 1 x 250㎍을 1 내지 10일간 정맥 주사.
b) 항 Id 1 X 50㎍을 11일째에 정맥 주사.
c) EDTA-Y90의 치료학적 용량을 14일째에 정맥 주사.
누드 마우스 및 종양 환자에 있어서 비교 면역 섬광 그래피 데이타를 기준으로 하면, 상기 섭생은 사람의 종양 치료요법에도 적절하다. 그러나, 사람 시스템에 있어서 주입될 양은 상당한 범위의 차이가 있다. 이중 특이적 수용체의 경우에는 10 X 5 내지 10g이고 항 Id의 경우에는 1 x 1g이다. 항 Id의 주사는 치료에 있어 불가피하다.
별첨 1a
DTPA 또는 EDTA 착물에 의한 MAb의 정량적 억제 ELISA
재료 : 분할가능한 96-웰 폴리스티렌 미세역가 플레이트(U 형) 타입 B(Nunc. no. 4-60445)
1) PBS(pH 7.2) 1ml중 접합체 1㎍ 농도의 Y-벤질-DTPA-HSA 19 접합체 50㎕를 각 웰에 피펫팅하고 실온(RT)에서 밤새 항온 처리한다.
2) 흡인 여과하여 상층액을 제거하고 0.05M 트리스시트레이트 완충액(pH 7.4)(세척용액 1)으로 3회 세척(1회 세척=웰당 세척용액 250㎕를 도입하고, 2분간 정치시킨 후, 흡입 여과)한다.
3) 미세 역가 플레이트가 즉시 필요하지 않는 경우, 셀룰로즈상에 실온에서 밤새 정치(아래를 개방하여)시킨다. 다음 플레이트를 건조 카트리지(Gaplast, Postfach 529, 8100 Garmisch-Partenkirchen 제조원)를 지닌 필름으로 밀봉한다. 이 플레이트를 상기 조건하에서 8주 이상 4℃에 유지시킬 수 있다.
4) 차단 용액 25㎕를 각 웰에 적용시킨 후 37℃에서 30분간 배양한다.
5) 차단중 희석한 하이브리도마 상층액을 컴피티터(competitor)와 함께 예비 배양한다(별첨 2 참조).
6) 적절히 예비 희석되고 예비 항온 처리된 시험용 하이브리도마 상층액 50㎕를 각 웰에 적응시킨 후 실온에서 30분간 배양한다.
7) 이어서, 세척 용액 2로 3회 연속하여 세척한다.
8) 이어서, 알칼리성 포스파타제로 표지하고 차단 용액중에 1 : 500로 희석시킨 염소 항-마우스 IgG1항체 50㎕를 각 웰에 적용시킨 후, 실온에서 30분간 배양한다.
9) Enzygnost용 세척 용액으로 3회 세척한다.
10) 이어서, 0.1mM NADP 50㎕를 가한다.
11) 실온에서 30분간 배양한다.
12) NADP와 함께 배양하는 동안, 다음과 같은 증폭 시스템이 형성된다 : 플레이트당 INT 2부 및 PBS(pH 7.2) 1부를 혼합한 후, 디아포라제 1부 및 ADH 1부를 피펫팅한다.
13) 이 시스템 50㎕를 각 웰에 넣는다.
14) 색상이 투명한 색에서 적색으로 확연히 변할 때, 웰당 0.1N H2SO4용액 100㎕를 가하여 반응을 정지시킨다.
15) TITRETEKRMULTiSCAN으로 492nm에서의 흡광도를 측정한다. 용액 50㎕와 함께 NADP 50㎕ 및 0.1N H2SO41200㎕를 블랭크로서 사용한다.
NADP-Sigma 품목번호 N-0505
INT-Sigma 품목번호 I-8377
ADH-Sigma 품목번호 A-3263
DIAPHORASE-Sigma 품목번호 D-2381
세척용액 2-Behring, 품목번호 OSEW96(Tween/PBS 함유)
차단용액 :
카제인을 가하고 30분간 교반하여 카제인중 3% 농도의 PBS(pH 7.2)를 제조하고, pH를 7.4로 조정한다. 4,000rpm에서 10분간 원심분리하여 입자를 제거한다.
희석된 염소 항-마우스 IgG1항체를 알칼리성 포스파타제(Southern Biotechnology로부터 입수, Cat. No. 1080-04)로 표지한다.
0.1mM NADP의 제조 :
NADP 7.65mg을 20mM 트리스, 0.1mM MgSO4(pH 9.5) 100ml중에 용해시킨다; 이 용액은 수개월간 -20℃에서 저장할 수 있다.
INT(P-요오도니트로테트라졸륨 바이올렛)의 제조 :
30% 에탄올 2.5mg/m을 초음파 욕에 용해시키고; 항상 신선하게 제조한다.
디아포라제(diaphorase)의 제조 : PBS(pH 7.2) ml당 디아포라제 1mg을 -20℃에서 부분적으로 저장한다.
알코올 디하이드로게나제의 제조 :
PBS(pH 7.2) ml당 ADH 0.5mg을 -20℃에서 부분적으로 저장한다.
별첨 1b
하이브리도마 상층액과 컴피티터와의 예비 항온 처리
시판용의 정량적 ELISA 시스템을 사용하여 하이브리도마 상층액중의 마우스 IgG 농도를 측정하며, 이는 문헌에 기술되어 있다.
ELISA 농도 측정을 기준으로 하여, 하이브리도마 상층액을 Ca++및 Mg++부재의 PBS 중 1.25㎍/ml으로 희석시킨다.
g을 mol로 전환 :
150,000g-MAb 1mol
1.25 x 10-6G-xmol
1.25㎍=x=8.33 x 10-12mol
MAb 및 억제제가 1+1의 비율을 갖도록 하기 위해, 인수 5에 의해 증가되는 8.33 x 10-12몰/200㎕ 농도의 억제제 10㎕를 8.33 x 10-22몰/ml 농도의 하이브리도마 상층액 50㎕에 가한다.
하이브리도마 상층액을 100,000배, 50,000배, 10,000배, 5,000배, 1,000배 및 100배 과량의 컴피티터와 함께 실온에서 30분간 배양한다. 이것 50㎕를 ELISA내에 피펫팅한다(별첨 1a, 6번 참조).
별첨 1c
DTPA 및 EDTA 착물의 제조
표 1에 나타낸 금속 이온에 대한 DTPA 및 EDTA의 착화 상수가 매우 높아서 DTPA 또는 EDTA와 상기 금속 이온의 등몰 혼합에 있어 완전한 포화가 예상되어야 한다. 이를 위해, 상응하는 금속 이온을 3배몰 과량으로 DTPA 및 EDTA와 함께 항온 처리시킨다. 실시예에서와 같이, 2회 증류시킨 물(별첨 1d 참조)중 10mM 황산카드뮴 용액 170㎕를 2회 증류시킨 물중 0.028몰의 DTPA 스톡 용액 30㎕와 함께 실온에서 5분간 항온 처리한다. 상기 컴피티터 용액 10㎕의 하이브리도마 상층액을 혼합하여 하이브리도마 상층액중에 함유된 MAb보다 100,000배 과량인 컴피티터를 얻는다. 목적하는 과량의 몰을 위해 특정한 염 이온용액중에서 컴피티터 용액을 적절하게 희석시킴으로써 MAb에 대한 컴피티터의 보다 낮은 비를 얻는다(별첨 Ib 참조).
별첨 1d
사용되는 금속 이온의 공급원 및 관련된 물리화학적 매개 변수
2회 증류시킨 물중에서 하기의 금속 이온 10밀리몰 용액을 제조한다 :
염화 제1마그네슘 분자량 161.88
(Merck) 번호 5934 Mn이온 반경 : 80pm
황산 카드뮴 분자량 256.5
(Riedel de Haen) 번호 31145 Cd이온 반경 : 77pm
염화아연 분자량 136.28
(Merck) 번호 8816 Zn이온 반경 : 74pm
황산구리 분자량 159.61
(Riedel de Haen) 번호 31294 Cu이온 반경 : 96pm
염화이트륨 분자량 303.36
(Aldrich) 번호 20,491-9 Y이온 반경 : 92pm
질산 납(II) 분자량 331.20
(Riedel de Haen) 번호 31137 Pb이온반경 : 120pm
별첨 1e
DTPA 및 EDTA에 의한 MAb 억제의 정량적 분석
고체상 항원에 대한 결합을 50% 억제하는 몰 과량의 컴피티터
Figure kpo00002
Figure kpo00003
Figure kpo00004
Figure kpo00005
Figure kpo00006
Figure kpo00007
Figure kpo00008
Figure kpo00009
Figure kpo00010
Figure kpo00011
[구조식 1]
Figure kpo00012
[구조식 2]
Figure kpo00013

Claims (11)

  1. a) 항원 결합 특이성을 갖는 제1항체의 VH 및 CH1 영역; b) 제1항체의 항원 결합 특이성과 상이한 항원 결합 특이성을 갖는 제2항체의 VH 및 CH1 영역; 및 c) 제1항체의 CH1 영역을 제2항체의 VH 영역에 항체의 경쇄 또는 항원 결합을 방해하지 않으면서 연결시키는 폴리펩타이드 스페이서로 이루어지는 니중 특이성 또는 올리고 특이성, 일가 또는 올리고가 수용체.
  2. 제1항에 있어서, 제1항체 및 제2항체의 경쇄를 추가로 포함하는 수용체.
  3. 제2항의 수용체를 포함하는, 종양 진단제
  4. 제2항에 있어서, 제1항체가 동물 또는 사람 종양-연관된 항원에 결합하는 수용체.
  5. 제2항에 있어서, 촉매 또는 효소 활성을 갖는 수용체.
  6. 제2항에 있어서, 제1항체가 동물 또는 사람 중앙-연관된 항원에 결합하고, 제2항체가 킬레이트에 결합하는 수용체.
  7. 제2항에 있어서, 제1항체의 가변 영역이 표 2, 표 3, 표 4 및 표 5에 나타낸 VH또는 VK의 아미노산 서열로 이루어지는 그룹으로부터 선택되는 VH또는 VK의 아미노산 서열을 포함하는 수용체.
  8. 제4에 있어서, 제1항체의 가변 영역이 표 2, 표 3, 표 4 및 표 5에 나타낸 VH또는 VK의 아미노산 서열로 이루어지는 그룹으로부터 선택되는 VH또는 VK의 아미노산 서열을 포함하는 수용체.
  9. 제5항에 있어서, 제1항체의 가변 영역이 표 2, 표 3, 표 4 및 표 5에 나타낸 VH또는 VK의 아미노산 서열로 이루어지는 그룹으로부터 선택되는 VH또는 VK의 아미노산 서열을 포함하는 수용체.
  10. 제6항에 있어서, 제1항체의 가변 영역이 표 2, 표 3, 표 4 및 표 5에 나타낸 VH또는 VK의 아미노산 서열로 이루어지는 그룹으로부터 선택되는 VH또는 VK의 아미노산 서열을 포함하는 수용체.
  11. 제2항의 수용체를 포함하는, 종양을 치료하기 위한 약제학적 조성물.
KR1019900009252A 1989-06-22 1990-06-22 이중특이성 및 올리고특이성 일가 및 올리고가 수용체 및 이를 포함하는 약제학적 조성물 KR0183980B1 (ko)

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EP0404097A3 (de) 1991-10-23
US5591828A (en) 1997-01-07
PT94443B (pt) 1997-02-28
CA2019559A1 (en) 1990-12-22
KR910001057A (ko) 1991-01-30
ES2093623T3 (es) 1997-01-01
AU5762190A (en) 1991-01-03
IE902254L (en) 1990-12-22
EP0404097A2 (de) 1990-12-27
AU639241B2 (en) 1993-07-22
DK0404097T3 (ko) 1997-02-10
ATE142230T1 (de) 1996-09-15
EP0404097B1 (de) 1996-09-04
PT94443A (pt) 1991-02-08
CA2019559C (en) 2002-01-08
RU2096459C1 (ru) 1997-11-20
DE59010480D1 (de) 1996-10-10
JP2978210B2 (ja) 1999-11-15
GR3021109T3 (en) 1996-12-31
JPH0348699A (ja) 1991-03-01
IE76715B1 (en) 1997-10-22
DE3920358A1 (de) 1991-01-17
IE902254A1 (en) 1991-01-16

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