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- W2049283516 abstract "A highly active elastolytic enzyme was isolated in addition to the well-known clastase (pancreatopeptidase E, EC 3.4.21.11), from a crude elastase preparation. The enzyme was partially purified and some of its physical and kinetic properties were determined. The approximate molecular weight was 21 900, the absorbance index (A1cm1%) at 282 nm was 20.5, and the pH optimum was 8.7. The apparent Km and kcat for elastolysis were 8.9 mg/ml, and 11.4 min−1, respectively. In addition to the elastolytic activity, the enzyme showed a considerable general proteolytic activity and very high activity towards N-acetyl-l-tyrosine ethyl ester and benzyloxycarbonyl-l-alanine p-nitrophenyl ester (NBA), which are all blocked by diisopropylfluorophosphate (DFP)." @default.
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- W2049283516 date "1974-04-01" @default.
- W2049283516 modified "2023-10-14" @default.
- W2049283516 title "Partial purification and properties of porcine pancreatic elastase II" @default.
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- W2049283516 doi "https://doi.org/10.1016/0005-2744(74)90224-1" @default.
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