Structural polypeptides of simian rotavirus SA11 and the effect of trypsin | Zendy

Romilio T. Espejo | Zendy; Susana López | Zendy; Carlos F. Arias | Zendy

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Structural polypeptides of simian rotavirus SA11 and the effect of trypsin

Author(s) -

Romilio T. Espejo,

Susana López,

Carlos F. Arias

Publication year - 1981

Publication title -

journal of virology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.617

H-Index - 292

eISSN - 1070-6321

pISSN - 0022-538X

DOI - 10.1128/jvi.37.1.156-160.1981

Subject(s) - trypsin , biology , rotavirus , simian , cleavage (geology) , reoviridae , molecular mass , biochemistry , virology , chymotrypsin , microbiology and biotechnology , virus , enzyme , paleontology , fracture (geology)

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.

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