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Title: [Alkaline DNAse from rat brain]. Author: Ivanov VA, Tret'iak TM, Gaziev AI, Santalov BF. Journal: Biokhimiia; 1980 May; 45(5):912-22. PubMed ID: 7378510. Abstract: A DNAse was isolated from rat brain and purified 1100-fold using affinity chromatography on a column with DNA-agarose and chromatography on granulated hydroxyapatite. The electrophoretically pure Mg2+, Mn2+-dependent enzyme preparation hydrolyzes the denaturated DNA with a maximal activity at pH 8,4. The optimal terminal concentration of Mg2+ corresponds to the Mg/phosphorus molar ratio of the substrate is 1:2. For Mn2+ this correlation is 1:1. Using the immobilized substrate method, the exonuclease type of DNAse activity has been established. The enzyme activity depends on the state of its SH-groups; the reaction is inhibited by pCMB. The molecular weight of DNAase as determined by gel-filtration through Sephadex G-200 is equal to 60 000.[Abstract] [Full Text] [Related] [New Search]