title: Complete amino acid sequence of the protease inhibitor from buckwheat seeds.
abstract: The complete amino acid sequence of protease inhibitor BWI-1 from buckwheat (Fagopyrum esculentum Moench) seeds has been established by automatic Edman degradation and mass spectrometry. The molecule of the inhibitor consists of 69 amino acid residues, with a molecular mass calculated as 7743.8 Da. The active site of the inhibitor contains an Arg45-Asp46 bond. Analysis of the amino acid sequence suggests that the buckwheat seed protease inhibitor is a member of the proteinase inhibitor I family.
authors.affiliation: A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.
authors.forename: M A
authors.initials: MA
authors.lastname: Belozersky
authors.forename: Y E
authors.initials: YE
authors.lastname: Dunaevsky
authors.forename: A X
authors.initials: AX
authors.lastname: Musolyamov
authors.forename: T A
authors.initials: TA
authors.lastname: Egorov
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002523:Edible Grain / Q000737:chemistry*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D012639:Seeds / Q000737:chemistry; D014361:Trypsin Inhibitors / Q000737:chemistry*
chemical_list: D000596:Amino Acids; C095816:BWI-1 protein, Fagopyrum esculentum; D010940:Plant Proteins; D014361:Trypsin Inhibitors