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- W2042529919 abstract "Chicken liver multicatalytic proteinase is composed of multiple components with molecular masses ranging from 23 to 34 kDa and has 'chymotrypsin-like' and 'trypsin-like' activities, which were examined by using the chromogenic peptide substrates, succinyl-Phe-Leu-Phe-pNA(p-nitroanilide) and N-benzoyl-Phe-Val-Arg-pNA, respectively. Treatment of the enzyme with diisopropyl fluorophosphate (DFP) completely abolished the 'chymotrypsin-like' activity, but had little effect on the 'trypsin-like' activity. In the experiment with radio-labeled DFP, SDS-PAGE of the modified enzyme revealed that the radioactivity was incorporated into only the smallest subunit (23 kDa). The migration of this subunit was retarded on SDS-PAGE after the treatment with DFP." @default.
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- W2042529919 date "1990-12-01" @default.
- W2042529919 modified "2023-10-02" @default.
- W2042529919 title "‘Chymotrypsin-like’ activity of chicken liver multicatalytic proteinase resides in the smallest subunit" @default.
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- W2042529919 doi "https://doi.org/10.1016/0167-4838(90)90283-l" @default.
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