title: The complete amino acid sequence of momordin-a, a ribosome-inactivating protein from the seeds of bitter gourd (Momordica charantia).
abstract: The complete amino acid sequence of momordin-a, a ribosome-inactivating protein from the seeds of bitter gourd, has been analyzed. Twenty-two peptides were isolated from the tryptic digest of momordin-a and sequenced by the DABITC/PITC double coupling method. The alignment of these tryptic peptides was done by analyzing the amino acid sequences of the peptides derived from chymotryptic digestion and cyanogen bromide cleavage of momordin-a as well as V8 protease-digestion of the CNBr fragment. Momordin-a consisted of 250 amino acid residues and carbohydrate residues attached to Asn227, and its molecular mass was calculated to be 28,690 Da. The sequence comparison with ricin A-chain shows that 33% of the residues of momordin-a are identical to those of ricin A-chain and that the residues involved in the catalytic site of the ricin A-chain are conserved in momordin-a.
authors.affiliation: Laboratory of Protein Chemistry and Engineering, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Minami
authors.forename: G
authors.initials: G
authors.lastname: Funatsu
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002240:Carbohydrate Sequence; D002851:Chromatography, High Pressure Liquid; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009699:N-Glycosyl Hydrolases; D010446:Peptide Fragments / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D054790:Ribosome Inactivating Proteins, Type 2; D012276:Ricin / Q000737:chemistry; D016415:Sequence Alignment
chemical_list: D000596:Amino Acids; D037102:Lectins; D010446:Peptide Fragments; D010940:Plant Proteins; D054790:Ribosome Inactivating Proteins, Type 2; D012276:Ricin; D009699:N-Glycosyl Hydrolases