Kaplan J C, Wilbert S M, Black P H
J Virol. 1972 May;9(5):800-3. doi: 10.1128/JVI.9.5.800-803.1972.
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.
纯化的猴病毒40与一种核酸内切酶活性相关,该酶可将I型(双链、环状)猴病毒40脱氧核糖核酸转化为带切口的形式,这种形式在碱性蔗糖梯度中以单一峰的形式沉降。该酶的活性依赖于镁离子,并且完全被乙二胺四乙酸(0.02 m)或加热(80℃处理10分钟)所抑制。在三(羟甲基)氨基甲烷 - 盐酸盐缓冲液中,它在37℃、pH 6.7至7.1之间表现出最佳活性。对纯化的、裂解的病毒进行凝胶电泳分析表明,未检测到可检测到的宿主细胞蛋白污染。