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Isolation and some properties of ATP-dependent DNAse from sea urchin (Strongylocentrotus intermedius) embryo

Gafurov, I.M.; Terent'ev, L.L.; Rasskazov, V.A.

Biokhimiia 44(6): 996-1004

1979

ISSN/ISBN: 0320-9725
PMID: 465608
Document Number: 149249
An ATP-dependent DNAse was isolated from the cells of sea urchin S. intermedius embryos by chromatography on DEAE-cellulose and gel chromatography on Sepharose 4B. The enzyme was found homogeneous during polyacrylamide gel electrophoresis. The MW of the enzyme was determined by gel filtration through Sepharose 6B and was .apprx. 450,000. The sedimentation coefficient as determined by ultracentrifugation was .apprx. 15S. The pH optimum during native DNA hydrolysis lies within the pH range of 6.5-9.0 and that during hydrolysis of denaturated DNA.sbd.within the pH range of 9.0-9.5. The enzyme was activated by ATP and dATP at the optimal concentration of 10-4 M. Other nucleoside triphosphates did not substitute for ATP in this reaction. The hydrolysis of denatured DNA occurred via the exonuclease way with a formation of short (di-, tri-, tetra- and penta-) oligonucleotides. The enzyme hydrolyzed native DNA according to the endonuclease type with predominant formation of high MW polynucleotides.

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