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- W2079186429 abstract "Abstract An extracellular acid ribonuclease produced by the mold Penicillium janthinellum has been purified 26-fold by a combination of selective heat treatment, ammonium sulphate precipitation and gel filtration on Sephadex G-200. The preparation gave a single band on electrophoresis on polyacrylamide gel at three different pH values. The enzyme has a pH optimum at 3.4. It is a heat-stable enzyme having no metal requirement but it is inhibited by divalent metal ions like Cu 2+ , Zn 2+ and Hg 2+ . It is a protein of mol. wt 30 000 and is not an -SH enzyme. It is a phosphotransferase catalyzing the hydrolysis of ribopolynucleotides to nucleoside-3′-monophosphates, via -2′,3′-cyclic mononucleotides. When -2′,3′-cyclic mononucleotides or homopolynucleotides are used as substrates the enzyme hydrolyses those containing uracil at a much faster rate than others." @default.
- W2079186429 created "2016-06-24" @default.
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- W2079186429 date "1974-09-01" @default.
- W2079186429 modified "2023-09-27" @default.
- W2079186429 title "Purification and properties of an extracellular acid ribonuclease from Penicillium janthinellum" @default.
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- W2079186429 doi "https://doi.org/10.1016/0005-2787(74)90375-x" @default.
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