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[野生型禽瘟病毒及其温度敏感突变体的M蛋白与禽瘟病毒核糖核蛋白在体外的相互作用]

[Interaction of the M protein of the wild-type fowl pest virus and its ts-mutant with the ribonucleoprotein of the fowl pest virus in vitro].

作者信息

Leneva I A, Mel'nikov S Ia, Mikheeva A V, Gendon Iu Z

出版信息

Vopr Virusol. 1985 Nov-Dec;30(6):711-4.

PMID:4095978
Abstract

The extent of inhibition of transcription realized in vitro by fowl plague virus (FPV) ribonucleoprotein (RNP) upon the addition of M protein isolated from FPV virions does not depend on nonionic detergent concentration in the reaction medium but does depend greatly on NaCl concentration. The highest inhibition of transcription is observed at a low ionic strength (0.02 M NaCl); inhibition is completely eliminated by increasing NaCl concentration to 0.3 M. When M protein isolated from FPV virions with ts mutation of M protein is added to RNP, addition to the system of 0.3 M NaCl decreases transcription inhibition but does not eliminate it completely.

摘要

通过添加从禽痘病毒(FPV)病毒粒子中分离出的M蛋白,在体外由禽痘病毒核糖核蛋白(RNP)实现的转录抑制程度并不取决于反应介质中的非离子洗涤剂浓度,而是极大地取决于NaCl浓度。在低离子强度(0.02M NaCl)下观察到最高的转录抑制;将NaCl浓度增加到0.3M可完全消除抑制作用。当将从具有M蛋白ts突变的FPV病毒粒子中分离出的M蛋白添加到RNP中时,向系统中添加0.3M NaCl可降低转录抑制,但不能完全消除。

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