| Literature DB >> 7006598 |
J K Shetty, R C Weaver, J E Kinsella.
Abstract
A ribonuclease (RNAase; EC 3.1.14.1) from brewer's yeast was purified 90-fold. Crude RNAase was initially separated from other proteins by precipitation at pH 4.0 after incubation of the mechanically disrupted yeast cells at pH 6.0 and 52 degrees C for 30 min. The RNAase was purified from the supernatant by ultrafiltration with a PM-30 membrane and adsorption chromatography on hydroxyapatite. RNAase preparation was free of phosphatase, deoxyribonuclease and phosphodiesterase activities. It showed maximum activity at pH 6.0 and a temperature optimum of 52 degrees C with yeast RNA as substrate. This RNAase hydrolysed yeast RNA to nucleoside 3'-phosphates and showed no evidence of base specificity.Entities:
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Year: 1980 PMID： 7006598 PMCID： PMC1162006 DOI： 10.1042/bj1890363
Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857