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- W1998691252 abstract "α-Glucosidase (EC 3.2.1.20) from Trichoderma viride was purified by a procedure including Sephacryl S-200 HR column chromatography, preparative isoelectric focusing, and Superdex 200 HR column chromatography. The enzyme was found to have an apparent molecular weight of 67,000 on SDS/PAGE and 65,000 on gelfiltration, showing that the enzyme is a single peptide. The isoelectric point of the enzyme was 5.0. The enzyme hydrolyzed α-1,4-glucosidic linkage more rapidly than α-1,6-glucosidic and α-1,3-glucosidic linkages. The enzyme was weakly inhibited by castanospermine." @default.
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- W1998691252 date "1995-01-01" @default.
- W1998691252 modified "2023-09-25" @default.
- W1998691252 title "Purification and Properties ofα-Glucosidase fromTrichoderma viride" @default.
- W1998691252 doi "https://doi.org/10.1271/bbb.59.2181" @default.
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