Complete amino acid sequences of two trypsin inhibitors from buckwheat seed.
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.
Pandya
M J
MJ
IACR-Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, U.K.
Smith
D A
DA
Yarwood
A
A
Gilroy
J
J
Richardson
M
M
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
C102121:BTI protein, Fagopyrum esculentum; D010446:Peptide Fragments; D010940:Plant Proteins; D014361:Trypsin Inhibitors