禽成髓细胞瘤病毒核心中受去污剂抑制的热不稳定核苷三磷酸酶
Detergent-inhibited, heat-labile nucleoside triphosphatase in cores of avian myeloblastosis virus.
作者信息
Jensen K F
出版信息
J Virol. 1978 Nov;28(2):427-33. doi: 10.1128/JVI.28.2.427-433.1978.
Abstract
Endogenous DNA synthesis was studied in isolated core particles of avian myeloblastosis virus. It was found that cores contained an enzymatic activity which rapidly converted the added nucleoside triphosphates to diphosphates (but not further) at 0 degrees C, thus inhibiting DNA synthesis. This triphosphatase probably originates from the viral membranes. In the cores the enzyme is completely inactivated by low concentrations (0.02%) of Nonident P-40. Also, the enzyme is very thermolabile and denatures rapidly at 38 degrees C.
摘要
对禽成髓细胞瘤病毒分离的核心颗粒中的内源性DNA合成进行了研究。发现核心颗粒含有一种酶活性，该活性在0℃时能迅速将添加的核苷三磷酸转化为二磷酸（但不会进一步转化），从而抑制DNA合成。这种三磷酸酶可能起源于病毒膜。在核心颗粒中，该酶会被低浓度（0.02%）的Nonident P - 40完全灭活。此外，该酶对热非常不稳定，在38℃时会迅速变性。
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