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pubmed:abstractText |
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.
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