Endonuclease activity associated with purified simian virus 40 virions.
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.
D002499:Centrifugation, Density Gradient; D004279:DNA, Viral / Q000032:analysis; D003851:Deoxyribonucleases / Q000302:isolation & purification*; D004492:Edetic Acid; D004586:Electrophoresis; D005782:Gels; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008274:Magnesium; D013539:Simian virus 40 / Q000201:enzymology*; D013395:Sucrose; D013997:Time Factors; D014316:Tritium; D014764:Viral Proteins / Q000032:analysis
D004279:DNA, Viral; D005782:Gels; D014764:Viral Proteins; D014316:Tritium; D013395:Sucrose; D004492:Edetic Acid; D003851:Deoxyribonucleases; D008274:Magnesium