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首页> 外文期刊>Journal of Virology >Virion-Bound Protein Kinase in Semliki Forest and Sindbis Viruses
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Virion-Bound Protein Kinase in Semliki Forest and Sindbis Viruses

机译：Semliki森林和Sindbis病毒中的病毒尼腺苷蛋白激酶

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摘要

Semliki forest virus and Sindbis virus (Alphaviruses belonging to the togavirus group) grown in BHK-21 cells possessed very low levels of virion-associated protein kinase activity. For comparison, vesicular stomatitis virus, also grown in BHK-21 cells, contained a virion-bound protein kinase which had a specific activity 80 times greater than that of the Alphaviruses. The Alphavirus protein kinase was unmasked by the nonionic detergent Nonidet P-40 but was not activated by cyclic nucleotides. Phosvitin was the best exogenous phosphate acceptor for assaying the viral enzyme in vitro. Phosphoprotein phosphatase activity was also detected in the Alphaviruses. Both in vivo and in vitro, all of the viral structural polypeptides were phosphorylated, and the phosphorylated amino acids were found to be serine and threonine. The viral nucleocapsid protein was about four times more efficient as a phosphate acceptor than were the envelope proteins. From 33 to 50% of the total protein kinase was bound to the viral nucleocapsid, and the specific activity of this enzyme was 4 to 10 times greater than that associated with the viral envelope.
机译：在BHK-21细胞中生长的Semliki森林病毒和属于Togavirus组的alphaviruses，具有非常低的病毒素相关蛋白激酶活性。为了比较，在BHK-21细胞中也生长的凹凸口炎病毒含有病毒素结合的蛋白激酶，其特异性活性比alphavirous的特定活性大80倍。 alphavirous蛋白激酶由非离子洗涤剂Nonidet p-40取消掩蔽，但未通过环状核苷酸激活。 Phosvitin是在体外测定病毒酶的最佳外源性磷酸盐受体。在甲烷烃中还检测磷蛋白磷酸酶活性。在体内和体外，所有病毒结构多肽都磷酸化，发现磷酸化的氨基酸是丝氨酸和苏氨酸。病毒核衣壳蛋白为磷酸盐受体的效率约为四倍，而不是包膜蛋白。从33至50％的总蛋白激酶与病毒核衣壳结合，并且该酶的比活性比与病毒包膜相关的4至10倍。

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    《Journal of Virology》 |1974年第6期|共9页
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    K. B. Tan; F. Sokol;

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  • 收录信息 美国《科学引文索引》(SCI);
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