Abstract
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.
MeSH Terms
Amino Acid Sequence
Antigens, Viral/metabolism
Extracellular Space/immunology
Membrane Glycoproteins
Peptides/analysis
Trypsin
Vesicular stomatitis Indiana virus/immunology
Viral Envelope Proteins
Viral Proteins/metabolism
Chemicals
Antigens, Viral
G protein, vesicular stomatitis virus
Membrane Glycoproteins
Peptides
Viral Envelope Proteins
Viral Proteins
Trypsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Irving R A
Ghosh H P
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15 references, click to expand
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