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Title: [Isolation and physico-chemical properties of homogenous nuclease from Serratia marcescens]. Author: Filimonova MN, Balaban NP, Sharipova FP, Leshchinskaia IB. Journal: Biokhimiia; 1980 Nov; 45(11):2096-104. PubMed ID: 6263367. Abstract: A simplified procedure for purification of nuclease from Serratia marcescens, including chromatography on DEAE- and phosphocellulose in a stationary regime has been developed. The method described results in a physically homogenous enzyme, which does not contain phosphatase, phosphodiesterase or proteinase admixtures. The molecular weight of the enzyme as determined by polyacrylamide gel electrophoresis is 33 000 +/- 10%. p-Chloromercurybenzoate (10(-2) M) completely inactivates the enzyme, while beta-mercaptoethanol (0,64 M) in the presence of 2 M urea causes only partial inactivation of the enzyme. Urea (4 or 7 M), when added to the reaction mixture, increases the enzyme activity 2,2-, 1,7- and 1,4-fold as compared to native, denaturated DNA and RNA, respectively.[Abstract] [Full Text] [Related] [New Search]