A rapid method for the isolation of ribonuclease from yeast (Saccharomyces carlsbergensis)
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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.
2005 ◽
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pp. 85-90
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2010 ◽
Vol 45
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pp. 1445-1449
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2020 ◽
Vol 82
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pp. 103-109
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pp. 2287-2299
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2004 ◽
Vol 39
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pp. 1993-1997
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