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PMID: 69719 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Proteins of Rous-associated virus type 61: polypeptide stoichiometry and evidence that glycoprotein gp35 is not a cleavage product of gp85.

Journal of virology ·Vol. 23 ·No. 1 ·1977-07-00 ·Pages 10-9

Mosser AG, Montelaro RC, Rueckert RR

Abstract

The two glycoproteins, gp85 and gp35, of Rous-associated virus type 61 (RAV-61), were isolated from radiolabeled virions by gel electrophoresis and digested with trypsin. The chromatographic profile of the gp35 digest revealed no peaks in common with that of gp85; therefore, the smaller glycoprotein is not a cleavage product of gp85. The stoichiometry of radiolabeled RAV-61 proteins was studied by quantitative gel filtration and gel electrophoresis. Among the 11 polypeptides identified were 4 minor ones, including the beta(p91) and alpha(p64) chains of reverse transcriptase and two unidentified chains, p76 and p35; the latter two were unmasked by removing the virions' surface glycoproteins with a protease, bromelain. Virions contained some 15 to 30 molecules of reverse transcriptase.

MeSH Terms
Animals Avian Leukosis Virus/analysis,enzymology Chick Embryo Culture Techniques Glycoproteins/analysis Peptides/analysis RNA-Directed DNA Polymerase/analysis Viral Proteins/analysis
Chemicals
Glycoproteins Peptides Viral Proteins RNA-Directed DNA Polymerase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Mosser A G
Montelaro R C
Rueckert R R
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40 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.23.1.10-19.1977
Published
1977-07-00
Pages
10-9
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC515794
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.23.1.10-19.1977 PMC Full Text View journal details
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