The capsid polypeptides of the 190 XXXX of Helminthosporium victoriae.

@entity47016 @entity46437 @entity3584 @entity95 @entity214 @entity32387
@entity214 -PAGE of the 190 @entity46437 of Helminthosporium victoriae, using a discontinuous buffer system, revealed two major capsid polypeptides of mol. wt. 88K and 83K (p88 and @entity32387 ) and a minor polypeptide, @entity47016 . Peptide mapping by both limited proteolysis and selective chemical cleavage showed @entity32387 and @entity47016 to be closely related to p88. The origin of @entity32387 / @entity47016 could not be explained by proteolysis of p88 during virus preparation and storage. In @entity95 reticulocyte lysates, denatured dsRNA directed the synthesis of a single major translation product which was identical to capsid polypeptide p88 on the basis of coelectrophoresis, immunoprecipitation and peptide mapping. No translation products comparable in size to @entity32387 or @entity47016 were detected in vitro. These data indicated that the capsid of the 190 @entity46437 is encoded by a single gene and verified the classification of the virus as a member of the family Totiviridae. Radioiodination of intact virus under conditions considered optimum for surface-specific iodination showed p88 to be more readily available for labelling than @entity32387 or @entity47016 . Furthermore, when Western blots of capsid polypeptides were reacted with an antiserum to @entity3584 -stabilized virus (190S-G), p88 was more reactive to 190S-G antibodies than was @entity32387 / @entity47016 . These results suggest p88 is external to @entity32387 / @entity47016 in the capsid.
