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- W2083644433 abstract "1. A proteolytic activity was enriched by gel chromatographic methods about 20 times compared to the original 27,000 g supernatant of a Brachionus homogenate. The fractions which contained this activity eluted at a position corresponding to a relative molecular mass of 28 kDa. 2. The protease activity from these fractions was further purified (up to 1700 times) by affinity chromatography using columns containing covalently bound casein, Brachionus protein or p-aminobenzamidine. By using the casein and the p-aminobenzamidine column successively the enzyme protein could be purified to such an extent that, on SDS-electrophoresis, a single band was obtained at a position corresponding to a relative molecular mass of 27–28 kDa. 3. The purified protease exhibits optimum activity at pH 8.5; the Km on reaction with N-benzoyl-l-arginine-p-nitroanilide is 0.064 mM, and its energy of activation 38 kJ M−1 K−1. Judging by its sensitivity to several protease inhibitors, this protease seems to be a trypsin-like serine endopeptidase which may function within the stomach of Brachionus plicatilis. 4. Within the 27,000 g supernatant of the Brachionus homogenate a component was detected which inhibits protease activity. The relative molecular mass of this protease inhibitor was estimated to be ca 74 kDa." @default.
- W2083644433 created "2016-06-24" @default.
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- W2083644433 date "1993-10-01" @default.
- W2083644433 modified "2023-09-25" @default.
- W2083644433 title "Characterization of a 27 kDa endopeptidase and detection of a proteinase-inhibitor in homogenates of Brachionus plicatilis (Rotifera)" @default.
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- W2083644433 doi "https://doi.org/10.1016/0305-0491(93)90313-t" @default.
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