Studies on the amino and carboxyl terminal amino acid sequences of reovirus capsid polypeptides (original) (raw)

Techniques are described for isolating several reovirus capsid polypeptides in amounts sufficient for determination of amino and carboxyl terminal amino acid sequences and fingerprinting. Among them are chromatography on CM-and DEAE-Sephadex in the presence of urea, and gel filtration on agarose A-15 m in the presence of sodium dodecyl sulfate. Using a combination of these procedures, and starting with either virions or cores, polypeptides ~3, ~2, and ~2 have been obtained essentially pure. Polypeptides Xl and x2 have been obtained as a mixture which has so far not been resolved. All reovirus capsid polypeptides except ~2 possess blocked amino terminal amino acid residues. The amino terminal amino acid sequence of polypeptide p2 is HJX-Pro-Gly-Gly-Val-Pro-. This suggests that polypeptide ~2 is derived from its precursor, polypeptide ~1, by cleavage of the amino terminal portion of the polypeptide chain. The carboxyl terminal regions of at least three of the five major reovirus capsid polypeptides are different. Polypeptide 03 ends in-(val,val,leu)-COOH; polypeptide ~2 in-leu-(arg, tyr, tyr)-Arg-COOH; and either one or both of the two polypeptides Xl and h2 terminate(s) in-Arg-COOH, the adjacent amino acid sequence being different from that of ~2.

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