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- W2022132362 abstract "A proteinase from the larval midgut of Vespa orientalis was purified by exchange chromatography on DEAE-Sephadex A-50 and gel filtration on Sephadex G-75. This purified enzyme was proved to be homogeneous by electrophoresis on a cellulose acetate membrane. The molecular weight was calculated to be 27,000 by gel filtration. Optimum pH for the hydrolysis of N-benzoyl-arginine-ethyl ester (BAEE) was 7·5 to 8·5, and optimum temperature with casein as a substrate was 60°C at pH 8·0 for 20 min. According to studies with synthetic inhibitors the hornet protease belongs to the ‘serine proteases’, being inhibited by phenylmethyl sulphonylfluoride (PMSF) and tosyl-lysyl chloromethane (TLCK). The hydrolysis of different amino acid ester bonds and the cleavage specificity on the B chain of oxidized insulin allow us to speak of a trypsin-like protease." @default.
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- W2022132362 date "1971-10-01" @default.
- W2022132362 modified "2023-09-27" @default.
- W2022132362 title "Purification and characterization of a trypsin-like proteinase from the midgut of the larva of the hornet, Vespa orientalis" @default.
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- W2022132362 doi "https://doi.org/10.1016/0022-1910(71)90143-0" @default.
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