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- W1970426196 abstract "Incubation of soluble proteins from rat lens with the protease calpain II caused the precipitation of beta-crystallin polypeptides. Two-dimensional electrophoresis and sequence analysis identified beta-crystallin polypeptides both before and after their precipitation by calpain II. beta-crystallin polypeptides precipitated by calpain were cleaved at their NH2-terminal extensions. These cleavage sites were similar to cleavage sites occurring in beta-crystallin polypeptides precipitated during formation of experimental cataract induced by an overdose of selenite. These data suggested that calpain II caused beta-crystallin insolubilization during cataract formation, and indicated that the process can be mimicked in vitro." @default.
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- W1970426196 date "1993-06-21" @default.
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- W1970426196 title "β‐Crystallins insolubilized by calpain II in vitro contain cleavage sites similar to β‐crystallins insolubilized during cataract" @default.
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- W1970426196 doi "https://doi.org/10.1016/0014-5793(93)80131-d" @default.
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