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The complete amino acid sequence of a major trypsin inhibitor from seeds of foxtail millet (Setaria italica).

Tashiro M., Asao T., Hirata C., Takahashi K., Kanamori M.

The complete amino acid sequence of a major trypsin inhibitor (FMTI-II) from seeds of foxtail millet (Setaria italica) was determined by analysis of peptides derived from the reduced and S-carboxymethylated protein by digestion with TPCK-trypsin and Staphylococcus aureus V8 protease. FMTI-II consists of 67 amino acid residues, including 10 half-cystine residues which are involved in 5 disulfide bridges in the molecule. The established sequence had a high degree of homology to Bowman-Birk type inhibitors from leguminous and gramineous plants. The trypsin reactive-site peptide bond in FMTI-II also appears to be Lys (16)-Ser (17) by comparison with these sequences.

J. Biochem. 108:669-672(1990) [PubMed] [Europe PMC]

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