Structural polypeptides of mammalian type C RNA viruses. Isolation and immunologic characterization of a low molecular weight polypeptide, p10.

Structural polypeptides of mammalian type C RNA viruses. Isolation and immunologic characterization of a low molecular weight polypeptide, p10.
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哺乳动物 C 型 RNA 病毒的结构多肽。

DOI:
10.1016/s0021-9258(17)33195-2
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发表时间:
1976
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
S. Aaronson
S. Aaronson
中科院分区:
--
文献类型:
--
作者:
M. Barbacid;J. Stephenson;S. Aaronson

文献摘要

被引文献

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用连续离子交换层析和分子大小测定技术纯化了几种哺乳动物C型RNA肿瘤病毒的低分子量多肽。其中包括一种分子量为10,000至11,000的多肽,p10,来自两种小鼠来源的C型病毒。Rauscher-和Moloney-鼠白血病病毒(穆尔病毒),以及来自毛猴的传染性C型病毒分离株。还纯化了这些病毒的p12结构多肽以及Rauscher-MuL病毒p15。通过使用针对每种多肽开发的放射免疫测定,可以证明所有三种低分子量多肽p15、p12和p10在免疫学上是独特的。在C型病毒结构多肽中,p10在免疫学上的特征最少。本研究的结果表明,p10是病毒编码的,并具有很强的组特异性抗原决定簇。通过使用适当的免疫测定,广泛反应的种间决定因素共享的哺乳动物C型病毒分离株的小鼠,猫,灵长类动物的起源,也被证明。p10的种间抗原决定簇显示出与C型病毒主要结构多肽p30一样广泛的交叉反应性。
Low molecular weight polypeptides of several mammalian type C RNA tumor viruses were purified by sequential ion exchange chromatography and molecular sizing techniques. These included a polypeptide with a molecular weight of 10,000 to 11,000, p 10, from two type C viruses of mouse origin. Rauscher- and Moloney-murine leukemia virus (MuL virus), and from an infectious type C virus isolate of the woolly monkey. The p12 structural polypeptides of these viruses as well as Rauscher-MuL virus p15 were also purified. By using radioimmunoassays developed for each polypeptide, it was possible to demonstrate that all three low molecular weight polypeptides, p15, p12, and p10, were immunologically unique. Among type C viral structural polypeptides, p10 has been least well characterized immunologically. The results of the present study indicate that p10 is virus-coded and possesses strong group-specific antigenic determinants. By use of appropriate immunoassays, broadly reactive interspecies determinants shared by mammalian type C virus isolates of murine, feline, and primate origin, were also demonstrated. The interspecies antigenic determinants of p10 were shown to be as broadly cross-reactive as those exhibited by the major type C virus structural polypeptide, p30.