Structural studies on the coat protein of alfalfa mosaic virus. Isolation and characterization of the tryptic peptides and the alignment of the cyanogen-bromide fragments.
The reduced and carboxymethylated coat protein of alfalfa mosaic virus (AMV 425) was fragmented by means of cyanogen-bromide cleavage. The tryptic peptides from the protein and its four cyanogen-bromide fragments were isolated on a preparative scale by combinations of column and paper separation techniques. The tryptic digest of the carboxymethylated protein contained 24 peptides and two free amino acids. All peptides have been characterized by amino acid analyses and end-group determinations. Together the tryptic peptides account for a total chain length of 228 amino acids. The data are in good agreement with previous reports from this laboratory.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D003488:Cyanogen Bromide; D000455:Medicago sativa; D009029:Mosaic Viruses / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D010942:Plant Viruses / Q000032:analysis*; D014357:Trypsin; D014764:Viral Proteins / Q000032:analysis*
D000596:Amino Acids; D010446:Peptide Fragments; D014764:Viral Proteins; D014357:Trypsin; D003488:Cyanogen Bromide