Abstract
Analysis of purified simian rotavirus has shown that it contains fewer structural polypeptide classes than previously reported. Two polypeptides (molecular weights, 62,000 and 28,000) commonly found in purified rotaviruses were, in fact, produced by cleavage of a larger structural polypeptide (molecular weight, about 88,000) by trypsin, which is usually employed to increase the yield of rotaviruses in tissue culture. Trypsin-uncleaved, double-shelled rotaviruses are probably composed of only five polypeptide classes; three in the inner layer, and two in the outer layer.
MeSH Terms
Electrophoresis, Polyacrylamide Gel
Peptides/analysis
Reoviridae/analysis
Rotavirus/analysis
Trypsin/pharmacology
Viral Proteins/analysis,classification,metabolism
Chemicals
Peptides
Viral Proteins
Trypsin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Espejo R T
López S
Arias C
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23 references, click to expand
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