Pepinsky R B, Vogt V M
J Virol. 1983 Feb;45(2):648-58. doi: 10.1128/JVI.45.2.648-658.1983.
We have developed procedures for the purification of a 6,000-dalton protein from avian myeloblastosis virus. This protein is a major component of avian myeloblastosis virus, accounting for over 7% of total protein, and thus is equimolar with the other internal structural proteins in virions. As described in the accompanying paper (Hunter et al., J. Virol. 45:885-888, 1983), the results of N-terminal amino acid sequence analysis identify the protein as a product of the gag gene. We suggest denoting this protein as p10, according to nomenclature that is already in use for a previously identified but poorly defined low-molecular-weight protein or proteins of avian sarcoma and leukemia viruses. In virions p10 appears to be located between the core and the membrane. Several of its properties may explain why p10 has not been characterized previously. Among these are its abnormal amino acid composition, its solubility under conditions where most proteins are fixed into sodium dodecyl sulfate-polyacrylamide gels, and the variability in its electrophoretic migration in different avian sarcoma viruses.
我们已经开发出了从禽成髓细胞瘤病毒中纯化一种6000道尔顿蛋白质的方法。这种蛋白质是禽成髓细胞瘤病毒的主要成分，占总蛋白的7%以上，因此与病毒粒子中的其他内部结构蛋白等摩尔。如随附论文（Hunter等人，《病毒学杂志》45:885 - 888，1983年）所述，N端氨基酸序列分析结果确定该蛋白质是gag基因的产物。根据已用于先前鉴定但定义不明确的禽肉瘤和白血病病毒低分子量蛋白质的命名法，我们建议将这种蛋白质命名为p10。在病毒粒子中，p10似乎位于核心和膜之间。它的一些特性可能解释了为什么p10以前没有被表征。其中包括其异常的氨基酸组成、在大多数蛋白质固定于十二烷基硫酸钠 - 聚丙烯酰胺凝胶的条件下的溶解性，以及在不同禽肉瘤病毒中其电泳迁移的变异性。
