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PMID: 4342047 Published · ppublish English Journal Article

Capsid polypeptides of mouse Elberfeld virus. I. Amino acid compositions and molar ratios in the virion.

Journal of virology ·Vol. 10 ·No. 3 ·1972-09-00 ·Pages 347-55

Stoltzfus CM, Rueckert R

Abstract

The four major polypeptide chains (alpha, beta, gamma, delta) constituting the capsid protein of mouse Elberfeld (ME) virus were isolated by preparative electrophoresis on polyacrylamide gels, and the amino acid composition of each chain was determined. In addition, the molecular weights of the smallest chains of ME virus, mengovirus, and poliovirus, which had previously been determined by gel electrophoretic methods, were redetermined by gel filtration chromatography in 6 m guanidine hydrochloride. Each was found to have a molecular weight about 7,300. Using the reevaluated molecular weights and the known amino acid compositions of the chains, the molar ratio of each chain in the ME virion was determined by quantitative analysis of the distribution of radioactivity in the electrophoretically separated chains of virus which had been specifically radiolabeled with leucine or with methionine. Equimolar proportions of all four chains were found in the virion.

MeSH Terms
Amino Acids/analysis Carbon Isotopes Chromatography, Gel Electrophoresis, Polyacrylamide Gel Encephalomyocarditis virus/analysis Leucine Mengovirus/analysis Methionine Methods Molecular Weight Peptides/analysis,isolation & purification Poliovirus/analysis Species Specificity Spectrophotometry Sulfur Isotopes Tritium Viral Proteins/analysis,isolation & purification
Chemicals
Amino Acids Carbon Isotopes Peptides Sulfur Isotopes Viral Proteins Tritium Methionine Leucine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Stoltzfus C M
Rueckert R
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24 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1972-09-00
Pages
347-55
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC356473
Subset
IM
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