The amino acid sequence of a Bowman-Birk type proteinase inhibitor from faba beans (Vicia faba L.).
The amino acid sequence of a Bowman-Birk type proteinase inhibitor (FBI) from seeds of faba bean (Vicia faba L.) was determined by analysis of peptide fragments generated by reduction and S-carboxymethylation of enzymatically modified inhibitors, which were obtained from native FBI by limited proteolysis with TPCK-trypsin or TLCK-chymotrypsin at pH 3.5. The established sequence showed that FBI is highly homologous with Vicia angustifolia inhibitor (VAI0 but lacks the portion corresponding to the C-terminal 9 amino acids of VAI. The trypsin reactive-site peptide bond in FBI was also indicated to be Lys(16)-Ser(17) and the chymotrypsin reactive-site peptide bond to be Tyr(42)-Ser(43) by limited proteolysis with TPCK-trypsin or TLCK-chymotrypsin and by sequence comparison with other Bowman-Birk type inhibitors.
Asao
T
T
Department of Food Sciences, Faculty of Home Economics, Mukogawa Women's University, Hyogo.
Imai
F
F
Tsuji
I
I
Tashiro
M
M
Iwami
K
K
Ibuki
F
F
D000595:Amino Acid Sequence; D001665:Binding Sites; D007887:Fabaceae / Q000737:chemistry*; D008969:Molecular Sequence Data; D010946:Plants, Medicinal; D011480:Protease Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid
D011480:Protease Inhibitors