[Alkaline DNAse from rat brain].
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.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002729:Chloromercuribenzoates / Q000494:pharmacology; D003851:Deoxyribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D004355:Drug Stability; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D051381:Rats
D002729:Chloromercuribenzoates; D008345:Manganese; D003851:Deoxyribonucleases; D008274:Magnesium
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