virus S (AfV-S) and virus F (AfV-F) 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. AfV-F contained one major (φ3) and two minor (φ1 and φ2) 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 AfV-F4 and AfV-S1a particles were found from sedimentation and diffusion coefficients to be 13.1 × 10 and 12.4 × 10 respectively. AfV-F capsid was estimated to contain 120 molecules of polypeptide φ3 and one molecule each of polypeptides φ1 and φ2, while AfV-S capsid was estimated to contain 120 molecules of polypeptide φ1.

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


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