劳氏相关病毒61型的蛋白质：多肽化学计量以及糖蛋白gp35并非gp85裂解产物的证据
Proteins of Rous-associated virus type 61: polypeptide stoichiometry and evidence that glycoprotein gp35 is not a cleavage product of gp85.
作者信息
Mosser A G, Montelaro R C, Rueckert R R
出版信息
J Virol. 1977 Jul;23(1):10-9. doi: 10.1128/JVI.23.1.10-19.1977.
Abstract
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.
摘要
通过凝胶电泳从放射性标记的病毒粒子中分离出劳斯相关病毒61型（RAV-61）的两种糖蛋白gp85和gp35，并用胰蛋白酶进行消化。gp35消化产物的色谱图谱显示与gp85的图谱没有共同峰；因此，较小的糖蛋白不是gp85的裂解产物。通过定量凝胶过滤和凝胶电泳研究了放射性标记的RAV-61蛋白的化学计量。在鉴定出的11种多肽中，有4种是次要的，包括逆转录酶的β（p91）和α（p64）链以及两条未鉴定的链p76和p35；通过用蛋白酶菠萝蛋白酶去除病毒粒子的表面糖蛋白，后两者得以显现。病毒粒子含有约15至30个逆转录酶分子。
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