Westenbrink F, Koornstra W, Bentvelzen P
Eur J Biochem. 1977 Jun 1;76(1):85-90. doi: 10.1111/j.1432-1033.1977.tb11572.x.
Solubilized polypeptides of the murine mammary tumor virus (MuMT virus) were chromatographed on a column of immobilised concanavalin A. The unbound viral material was rechromatographed on phosphocellulose, resulting in the isolation of the major proteins with a molecular weight of 28000 (p28) and 12000 (p12) respectively. The adsorbed glycopolypeptides after elution with methyl alpha-D-mannopyranoside were subjected to gel filtration. The major glycoprotein with a molecular weight of 52000 (gp52) was obtained in an almost pure form. However, a considerable part of gp52 elutes together with a glycoprotein with a molecular weight of 36000 (gp36), suggesting that in addition to the free form of gp52 a complex exists of gp52 plus gp36.
将小鼠乳腺肿瘤病毒（MuMT病毒）的可溶性多肽在固定化伴刀豆球蛋白A柱上进行层析。未结合的病毒物质在磷酸纤维素上重新层析，分别分离出分子量为28000（p28）和12000（p12）的主要蛋白质。用α-D-甲基甘露糖苷洗脱后得到的吸附糖多肽进行凝胶过滤。获得了几乎呈纯形式的分子量为52000（gp52）的主要糖蛋白。然而，相当一部分gp52与分子量为36000（gp36）的糖蛋白一起洗脱，这表明除了gp52的游离形式外，还存在gp52加gp36的复合物。
