The complete amino acid sequence of a major trypsin inhibitor from seeds of foxtail millet (Setaria italica) |
| |
| Authors: | M Tashiro T Asao C Hirata K Takahashi M Kanamori |
| |
| Affiliation: | Department of Food Science and Nutrition, Faculty of Living Science, Kyoto Prefectural University. |
| |
| Abstract: | 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. |
| |
| Keywords: | |
|
