Abstract
The electrophoretic analysis of reovirus-specific polypeptides in infected cells using a discontinuous gel system has allowed the resolution of additional viral-specific polypeptides, including one large-sized gamma3 and two (or possibly three) medium-sized (mu3, mu4, mu5(?)) species. The proteins designated mu0, sigma1, and sigma2 based on electrophoretic mobility in gel systems containing phosphate-urea correspond to mu4, sigma2, and sigma1, respectively, when analyzed in systems containing Tris-glycine. It is likely that protein modifications (phosphorylation and glycosylation) are responsible for at least some of these differences.
MeSH Terms
Acetone
Buffers
Chemical Precipitation
Electrophoresis, Polyacrylamide Gel/methods
Glycine
Immune Sera
L Cells
Mammalian orthoreovirus 3/analysis
Peptides/analysis
Phosphates
Reoviridae/analysis
Tromethamine
Urea
Viral Proteins/analysis
Chemicals
Buffers
Immune Sera
Peptides
Phosphates
Viral Proteins
Tromethamine
Acetone
Urea
Glycine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Cross R K
Fields B N
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30 references, click to expand
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