Isolation and characterization of a trypsin inhibitor from finger millet

Manjunath, N.H. and Veerabhadrappa, P S and Virupaksha, T.K. (1983) Isolation and characterization of a trypsin inhibitor from finger millet. Phytochemistry, 22 (11). pp. 2349-2357.

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Abstract

A trypsin inhibitor (FMTI) isolated from Eleusine coracana had a mol. wt. of 12 000 and amino acid analysis showed that it contained 8 half-cystines and was rich in basic amino acids and glutamic acid. Glutamic acid was the N-terminal amino acid of the inhibitor. FMTI possessed the unique property of inhibiting α-amylases. FMTI in 1:1 complex with bovine trypsin exhibited α-amylase inhibitory activity suggesting the 'double-headed' nature of the inhibitor. The chemical modification of lysine and arginine residues indicated that -NH2 groups are essential for the activity of FMTI towards trypsin

Item Type: Article
Author Affiliation: Department of Chemistry, Central College, Bangalore University, Bangalore 560 001, India,Department of Biochemistry, University of Agricultural Sciences, GKVK Campus, Bangalore 560 065, India
Subjects: Plant Production
Crop Improvement
Divisions: Millet
Depositing User: Mr. SanatKumar Behera
Date Deposited: 18 May 2012 05:23
Last Modified: 18 May 2012 05:24
Official URL: http://dx.doi.org/10.1016/0031-9422(83)80119-8
URI: http://eprints.icrisat.ac.in/id/eprint/5463

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