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- W2053862558 abstract "Cathepsin D was highly purified from the skeletal muscle of Japanese monkey (Macacafuscatafuscata) by a procedure including affinity chromatography on concanavalin A-Sepharose and pepstatin-Sepharose, and then resolved into ten isozymes (A through J) by isoelectric focusing. When examined for specificity toward oxidized insulin B chain, isozyme A was highly specific and cleaved exclusively the Leu15-Tyr16 bond, whereas isozyme F was less specific, cleaving the Leu15-Tyr16 and Glu13-Ala14 bonds, with slower cleavages at several other bonds. These results demonstrate for the first time the occurrence of isozymes with different specificities among cathepsin D isozymes obtained from a single source." @default.
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- W2053862558 date "1991-04-01" @default.
- W2053862558 modified "2023-10-17" @default.
- W2053862558 title "Occurrence of cathepsin D isozymes with different specificities in monkey skeletal muscle" @default.
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- W2053862558 doi "https://doi.org/10.1016/s0006-291x(05)80256-6" @default.
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