title: Complete amino acid sequences of two trypsin inhibitors from buckwheat seed.
abstract: The major trypsin isoinhibitors from seed extracts of buckwheat (Fagopyrum esculentum Mönch) were purified by affinity chromatography, anion exchange chromatography, anion exchange HPLC and reversed-phase HPLC, and the complete amino acid sequences of two isoinhibitors, BTI-1 and BTI-2, were established by automated Edman degradation. Each isoinhibitor consists of a single polypeptide chain of 69 amino acids, including two Cys residues. The N-terminal sequence of a third isoform, BTI-3, was also determined. The buckwheat trypsin isoinhibitors exhibit clear sequence similarities with the potato chymotrypsin inhibitor I family of serine proteinase inhibitors.
authors.affiliation: IACR-Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, U.K.
authors.forename: M J
authors.initials: MJ
authors.lastname: Pandya
authors.forename: D A
authors.initials: DA
authors.lastname: Smith
authors.forename: A
authors.initials: A
authors.lastname: Yarwood
authors.forename: J
authors.initials: J
authors.lastname: Gilroy
authors.forename: M
authors.initials: M
authors.lastname: Richardson
mesh_terms: D000595:Amino Acid Sequence; D002523:Edible Grain / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: C102121:BTI protein, Fagopyrum esculentum; D010446:Peptide Fragments; D010940:Plant Proteins; D014361:Trypsin Inhibitors