The coat protein of particles of sweet potato feathery mottle potyvirus (SPFMV) extracted from spp. migrated in SDS-PAGE mainly as bands of 38 000 (38K), 36K, 32K and 30K. Trypsin treatment of the particles resulted in the appearance of only one 30K polypeptide. The inclusion of protease inhibitors in the extraction procedure did not alter the heterogeneity of SPFMV coat protein. A partially purified fraction of extracts from recovering, symptomless, but not from healthy leaves of had a proteolytic activity similar to that of trypsin. Amino acid sequencing showed that the trypsin-cleaved 30K polypeptide had some sequence homology with other potyvirus coat proteins. The site at which the extract cleaved the protein was five amino acids nearer the N terminus than the trypsin cleavage site.


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