1887

Abstract

SUMMARY

virus () and virus () have been shown to be serogically unrelated. Amino acid compositions of the two virus capsids are compared and their capsid polypeptides have been examined by SDS-polyacrylamide gel electrophoresis. contained one major (Ø3) and two minor (Ø1 and Ø2) polypeptides with mol. wt. 87000, 125000 and 100000, while AfV-S contained one major (σ1) and one minor (σ2) polypeptide with mol. wt. 83000 and 78000 respectively. Evidence is presented that σ2 may be derived from σ1 polypeptide by proteolytic degradation . The mol. wt. of 4 and -S1a particles were found from sedimentation and diffusion coefficients to be 13.1 × 10 and 12.4 × 10 respectively. capsid was estimated to contain 120 molecules of polypeptide Ø3 and one molecule each of polypeptides Ø1 and Ø2, while capsid was estimated to contain 120 molecules of polypeptide Ø1.

It has been shown that S1a and S2a particles each contain a molecule of double-stranded with mol. wt. 2.24 × 10 (-224) and 2.76 × 10 (-276) respectively, whereas S1b and S2b particles each contain a molecule of -224 and -276 respectively, together with an additional molecule of double-stranded of mol. wt. 0.1 × 10. Evidence is presented that S4 particles contain two molecules of -224. S3 particles gave only -224 on extraction, but contain the equivalent of 1½ molecules of -224; the nature of these particles and other possible virus replicative intermediates is discussed. Double-stranded of mol. wt. 1.24 × 10 was derived from a newly described particle class, Fo.

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1975-05-01
2024-04-27
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