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- W1997085953 abstract "Cathepsin D was purified 900-fold with 30% recovery from rabbit testes using pepstatin bound Sepharose affinity chromatography. The enzyme is homogeneous as observed by acrylamide gel electrophoresis. The heat stable enzyme exhibits an apparent molecular weight of 42,000 with identical subunits of 20,000. Purified cathepsin D catalyses the conversion of proacrosin to acrosin." @default.
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- W1997085953 date "1982-11-01" @default.
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- W1997085953 title "Isolation of rabbit testicular cathepsin D and its role in the activation of proacrosin" @default.
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- W1997085953 doi "https://doi.org/10.1016/0006-291x(82)91566-2" @default.
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