PURIFICATION AND CHARACTERIZATION OF A MAJOR GLYCOPROTEIN OF THE MURINE MAMMARY-TUMOR VIRUS

被引：6
作者：
WESTENBRINK, F
KOORNSTRA, W
机构：
[1] Radiobiological Institute TNO, Rijswijk
来源：
ANALYTICAL BIOCHEMISTRY | 1979年 / 94卷 / 01期
关键词：
D O I：
10.1016/0003-2697(79)90787-5
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Affinity chromatography of solubilized murine mammary tumor virus on concanavalin A-Sepharose was clearly affected by different mixtures of detergent present in the elution buffer: A complex consisting of a glycoprotein of 52,000 daltons (gp52), and a glycoprotein of 36,000 daltons (gp36), besides free gp52 were isolated. The gp36 could be purified by gel filtration of the complex in the presence of a high concentration of sodium deoxycholate. The elution of gp36 in the void volume of the Sephadex column and the results obtained with sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed strong hydrophobic interactions within the molecule. The glycoprotein was immunochemically characterized by competitive radioimmunoassay and immunoelectrophoresis. No cross-reactivity of gp36 with gp52 or two nonglycosylated viral polypeptides was observed. © 1979.
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页码：40 / 47
页数：8
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