title: The primary structure of papaya mosaic virus coat protein: a revision.
abstract: The presence of an acetyl blocking group at the N-terminus of the coat protein of papaya mosaic virus has been identified by FAB mass spectrometry. Furthermore, we have found that the N-terminal sequence of the protein is four amino-acid residues (AC-Ser-Lys-Ser-Ser-) longer than that previously reported, while Glu instead of Gln is the C-terminal residue. The present paper shows that PMV-protein is made up of 215 amino acid residues, with a molecular mass of 22,960 Da.
authors.affiliation: Dipartimento di Chimica Organica e Biologica, Universita' di Napoli, Italy.
authors.forename: C
authors.initials: C
authors.lastname: Verde
authors.forename: A
authors.initials: A
authors.lastname: Malorni
authors.forename: A
authors.initials: A
authors.lastname: Parente
mesh_terms: D000595:Amino Acid Sequence; D002213:Capsid; D003488:Cyanogen Bromide; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009029:Mosaic Viruses / Q000032:analysis*; D010446:Peptide Fragments; D014357:Trypsin
chemical_list: D010446:Peptide Fragments; D014357:Trypsin; D003488:Cyanogen Bromide