Journal
PEPTIDES
Volume 32, Issue 6, Pages 1151-1158Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2011.03.015
Keywords
Fagopyrum tartaricum; Trypsin inhibitor; Phytopathogenic fungi; Purification
Funding
- Committee of Science and Technology in Sichuan Province, China [2010HH0040]
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A major trypsin inhibitor was isolated and characterized from the seeds of the tartary buckwheat (Fagopyrum tataricum)(FtTI) by ammonium sulfate precipitation, ion exchange chromatography and centrifugal ultrafiltration. SDS-PAGE analysis under reducing condition showed that FtTI is a single polypeptide chain with a molecular mass of approximately 14 kDa. The complete amino acid sequence of FtTI was established by automatic Edman degradation and mass spectrometry. It was found that the trypsin inhibitor molecule consists of 86 amino acid residues containing two disulfide bonds which connect Cys(8) to Cys(65) and Cys(49) to Cys(58). The active site of the inhibitor was found to contain an Asp(66)-Arg(67) bond. MALDI-TOF analysis showed that FtTI has two isoforms (Mr: 11.487 and 13.838 kDa). Dixon plots revealed a competitive inhibition of trypsin with inhibition constants (Ki) of 1.6 nM. Analysis of the amino acid sequence suggests that FtTI is a member of the protease inhibitor I family. What is more, FtTI exhibited strong inhibitory activity against phytopathogenic fungi. (C) 2011 Elsevier Inc. All rights reserved.
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