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J Virol. 1972 May; 9(5): 800-803
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Endonuclease Activity Associated with Purified Simian Virus 40 Virions

¹ Department of Medicine, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts 02114

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.