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- W2000363603 abstract "Prolylcarboxypeptidase (angiotensinase C) was purified 247-fold from homogenized hog kidney cortex by the sequential application of ammonium sulfate precipitation. DEAE-Sephadex and hydroxylapatite column chromatographies. The enzyme was relatively heat stable and free of cathepsin A contamination. Disc gel electrophoresis revealed only a single band of protein indicating homogeneity. The molecular weight of the enzyme was estimated to be 210 000. The Km of prolylcarboxypeptidase with Bz-Pro Phe substrate was 1.3·10-3 M. After pretreatment with 2-mercaptoethanol, urea and sodium dodecyl sulfate prolylcarboxypeptidase dissociated to subunits." @default.
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- W2000363603 date "1973-03-01" @default.
- W2000363603 modified "2023-10-10" @default.
- W2000363603 title "Purification of lysosomal prolylcarboxypeptidase angiotensinase C" @default.
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- W2000363603 doi "https://doi.org/10.1016/0005-2744(73)90021-1" @default.
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