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Purification of a 17,000-Dalton Inhibitor of Ca2+_Activated Protease from Neoplastic Tissues of Human Stomach

한국동물학회지 1988년 31권 4호 p.295 ~ 299
설재홍, 박상철, 하두봉, 정진하,
소속 상세정보
설재홍 ( Seol Jae-Hong ) - 서울대학교 자연대학 동물학과
박상철 ( Park Sang-Chul ) - 서울대학교 의과대학 생화학교실
하두봉 ( Ha Doo-Bong ) - 서울대학교 자연대학 동물학과
정진하 ( Chung Chin-Ha ) - 서울대학교 자연대학 동물학과

Abstract


An endogenous 17-6a inhibitor of Caa+_activated protease has been purified from neo-plastic tissues of human stomach using heat treahent and conventional chromatographir procedures. It appears to consist of a single polvpeptide since the same molecular weight was obtained by both gel fntration under nondenaturing condition and gel electrophoresis in the presence of SDS. Since the size of the inhibitor or is the smallest amens those reported so far, it may represent a functional unit for inhibiting Caa+_activated protease. This protein is also capable of inhibiting the protease isolated loom chick skeletal muscle. Thus, the functional unit of the inhibitor most well be conserved during evolution. Howrver, it remains unclear what may be the physiological significance of the presence of the Iow-molecular weight form of the inhibitor in neoplastic tissues of human stomach.

키워드

Calpain ; Calpastatin ; Stomach tumor

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