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- W3148199621 abstract "Three active forms of autolyzed porcine trypsin, delta-, gamma- and sigma-trypsins, have been isolated by affinity chromatography on soybean trypsin inhibitor STI-Sepharose column. All these active forms are of the same molecular weight as the parent molecule beta-trypsin. When they react with specific substrates, their Michaelis constants, K_m, are almost the same as that of beta-trypsin. However, when treated with the specific inhibitor, soybean trypsin inhibitor, the inhibition constants, K_i of delta-, gamma- and sigma-trypsins, are apparently different from that of beta-trypsin." @default.
- W3148199621 created "2021-04-13" @default.
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- W3148199621 date "1986-01-01" @default.
- W3148199621 modified "2023-09-25" @default.
- W3148199621 title "AFFINITY CHROMATOGRAPHIC SEPARATION AND KINETIC PROPERTIES OF THE ACTIVE PRODUCTS OF PORCINE TRYPSIN AFTER AUTOLYSIS" @default.
- W3148199621 hasPublicationYear "1986" @default.
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