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首页> 外文期刊>Journal of Virology >Proteins of Rous-associated virus type 61: polypeptide stoichiometry and evidence that glycoprotein gp35 is not a cleavage product of gp85.
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Proteins of Rous-associated virus type 61: polypeptide stoichiometry and evidence that glycoprotein gp35 is not a cleavage product of gp85.

机译：蛋白质的蛋白质相关病毒型61：多肽化学计量和糖蛋白GP35不是GP85的切割产物的证据。

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摘要

The two glycoproteins, gp85 and gp35, of Rous-associated virus type 61 (RAV-61), were isolated from radiolabeled virions by gel electrophoresis and digested with trypsin. The chromatographic profile of the gp35 digest revealed no peaks in common with that of gp85; therefore, the smaller glycoprotein is not a cleavage product of gp85. The stoichiometry of radiolabeled RAV-61 proteins was studied by quantitative gel filtration and gel electrophoresis. Among the 11 polypeptides identified were 4 minor ones, including the beta(p91) and alpha(p64) chains of reverse transcriptase and two unidentified chains, p76 and p35; the latter two were unmasked by removing the virions' surface glycoproteins with a protease, bromelain. Virions contained some 15 to 30 molecules of reverse transcriptase.
机译：通过凝胶电泳从放射性标记的病毒粒子中分离出来的两种糖蛋白，GP85和GP35，从放射性标记的病毒中分离，并用胰蛋白酶消化。 GP35消化的色谱分布揭示了GP85的峰的峰;因此，较小的糖蛋白不是GP85的切割产物。通过定量凝胶过滤和凝胶电泳研究了放射性标记Rav-61蛋白的化学计量。在鉴定的11个多肽中，鉴定为4个次要的多肽，包括β（p91）和逆转录酶的α（p64）链和两个未识别的链，p76和p35;通过用蛋白酶，菠萝蛋白酶除去病毒粒子表面糖蛋白，后两者是未掩蔽的。病毒粒子含有约15至30分子的逆转录酶。

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