Abstract
The electrophoretic analysis of reovirus-specific polypeptides in infected [mouse L] cells using a discontinuous gel system allowed the resolution of additional viral-specific polypeptides, including 1 large-sized .lambda.3 and 2 (or possibly 3) medium-sized [.mu.3, .mu.4, .mu.5?] species. The proteins designated .mu.0, .sigma.1 and .sigma.2 based on electrophoretic mobility in gel systems containing phosphate-urea correspond to .mu.4, .sigma.2 and .sigma.1, respectively, when analyzed in systems containing Tris-glycine. Protein modifications (phosphorylation and glycosylation) may be responsible for at least some of these differences.