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- W2069712647 abstract "Ribonuclease was purified to homogeneity from Monascus sp. No. 3403 by column chromatography on DEAE-cellulose, DEAE-Toyopearl 650S, 5′-AMP Sepharose 4B, and Sephadex G-75. The molecular weight of the purified enzyme was estimated to be 30,000 by gel filtration and 26,000 by Sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme contained 5.0% carbohydrate. Homopolyadenylic acid was a good substrate for the enzyme. The optimum pH of the enzyme was 4.2 and its optimum temperature was 55°C." @default.
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- W2069712647 date "1995-01-01" @default.
- W2069712647 modified "2023-09-24" @default.
- W2069712647 title "Purification and Properties of a Ribonuclease from a Species of the GenusMonascus" @default.
- W2069712647 doi "https://doi.org/10.1271/bbb.59.327" @default.
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