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. 1972 May;9(5):800–803. doi: 10.1128/jvi.9.5.800-803.1972

Endonuclease Activity Associated with Purified Simian Virus 40 Virions

Joan C Kaplan 1, Sharon M Wilbert 1, Paul H Black 1
PMCID: PMC356376  PMID: 4337165

Abstract

Purified simian virus 40 has associated with it an endonuclease activity which converts form I (double-stranded, circular) simian virus 40 deoxyribonucleic acid to a nicked form that sediments as a homogeneous peak in alkaline sucrose gradients. The enzyme is dependent on magnesium ions for activity and is completely inhibited by ethylenediaminetetraacetic acid (0.02 m) or heat (80 C for 10 min). In tris(hydroxymethyl)aminomethane-hydrochloride buffer it exhibits optimal activity between pH 6.7 and 7.1 at 37 C. Gel electrophoretic analysis of purified, disrupted virus indicates the absence of detectable host cell protein contamination.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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