Irving R A, Ghosh H P
J Virol. 1982 Apr;42(1):322-5. doi: 10.1128/JVI.42.1.322-325.1982.
A comparison of partial NH2-terminal sequences of vesicular stomatitis viral glycoprotein G (molecular weight, 69,000) and the soluble extracellular glycoprotein antigen Gs (molecular weight, 57,000) shows that both of the sequences are identical. Tryptic fingerprint analyses show that Gs lacks the carboxy-terminal region containing the membrane-anchoring hydrophobic domain of G. These results suggest that Gs is formed by cleavage in the carboxy-terminal region of G.
水疱性口炎病毒糖蛋白G(分子量69,000)与可溶性细胞外糖蛋白抗原Gs(分子量57,000)的部分氨基末端序列比较表明,这两个序列是相同的。胰蛋白酶指纹分析表明,Gs缺乏包含G的膜锚定疏水结构域的羧基末端区域。这些结果表明,Gs是由G的羧基末端区域裂解形成的。