The complete amino acid sequence of rice bran trypsin inhibitor.
The complete amino acid sequence of a double-headed trypsin inhibitor (RBTI) from rice bran was determined by a combination of limited proteolysis of the native inhibitor with Streptomyces griseus trypsin at pH 3 and conventional methods. RBTI consists of 133 amino acid residues including 18 half-cystine residues which are involved in 9 disulfide bridges in the molecule. The limited proteolysis at pH 3 produced a major split of Lys(83)-Met(84) and a minor split of Arg(107)-Val(108) together with a non-enzymatic hydrolysis of Asp(19)-Pro(20) in the molecule. The established sequence showed that RBTI is composed of 4 domains, domains I and III, and domains II and IV being homologous to the first and the second domains of soybean Bowman-Birk inhibitor, respectively, indicating that RBTI has a duplicated structure of the Bowman-Birk type inhibitor.
Tashiro
M
M
Department of Food Science and Nutrition, Faculty of Living Science, Kyoto Prefectural University.
Hashino
K
K
Shiozaki
M
M
Ibuki
F
F
Maki
Z
Z
D000595:Amino Acid Sequence; D004220:Disulfides / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis; D014361:Trypsin Inhibitors
D004220:Disulfides; D010446:Peptide Fragments; D014361:Trypsin Inhibitors