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. 1987 Aug;102(2):297-306.
doi: 10.1093/oxfordjournals.jbchem.a122054.

The complete amino acid sequence of rice bran trypsin inhibitor

M Tashiro  1 , K Hashino, M Shiozaki, F Ibuki, Z Maki
Affiliations
Free article

The complete amino acid sequence of rice bran trypsin inhibitor

M Tashiro et al. J Biochem. 1987 Aug.
Free article

Abstract

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.

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