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KMID : 0364219880310040295
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Korean Journal of Zoology
1988 Volume.31 No. 4 p.295 ~ p.299
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Purification of a 17,000-Dalton Inhibitor of Ca2+_Activated Protease from Neoplastic Tissues of Human Stomach
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Seol Jae-Hong
Park Sang-Chul
Ha Doo-Bong
Chung Chin-Ha
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Abstract
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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.
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KEYWORD
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Calpain , Calpastatin , Stomach tumor
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