A mutant of the virus of foot-and-mouth disease (O type) was studied, and shown by electrophoresis in SDS-polyacrylamide gels to contain equimolar proportions of four polypeptides with mol. wts. of 34, 20, 17 and 14 × 10. Two minor components were also present with mol. wts. of 51 and 25 × 10 and in the molar ratio of 0.07 and 0.28. Only the polypeptide of mol. wt. 34 × 10 was labelled when the intact virus was iodinated. This polypeptide was sensitive to the action of trypsin and showed leucine as the -terminal amino acid. Our own and other results are discussed in terms of virus structure.


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