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- W2086553693 abstract "1. A ribonuclease from bovine aorta has been partially purified. 2. The purification procedure involved ethanol fractionation and gel filtration on polyacrylamide and Sephadex. 3. The enzyme is free of deoxyribonuclease, phosphomonoesterase, and cyclic phosphatase activity (under the conditions employed). It exhibited a small amount of diesterase activity using bis (p-nitrophenyl) phosphate as substrate. 4. A comparison of the action of the enzyme on poly (C), poly (A), poly (U), poly (I) and RNA with the action of bovine pancreatic ribonuclease is presented. 5. The optimum temperature for activity was about 50° and optimum pH about 7.0." @default.
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- W2086553693 date "1967-09-01" @default.
- W2086553693 modified "2023-09-27" @default.
- W2086553693 title "Bovine aorta ribonuclease" @default.
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- W2086553693 doi "https://doi.org/10.1016/0005-2787(67)90044-5" @default.
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