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Double-headed trypsin/chymotrypsin inhibitors from horse gram (Dolichos biflorus): purification, molecular and kinetic properties.

Sreerama, Y. N. and Das, J. R. and Rao, D. R. and Gowda, L. R. (1997) Double-headed trypsin/chymotrypsin inhibitors from horse gram (Dolichos biflorus): purification, molecular and kinetic properties. Journal of Food Biochemistry, 21 (6). pp. 461-477.

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Abstract

Four proteinase inhibitors were purified to homogeneity from horse gram (Dolichos biflorus). These inhibitors are double-headed and inhibit trypsin and chymotrypsin simultaneously and independently. Dissociation constants range between 0.87 and 4.6 x 10-7M. Each of the 6 isoinhibitors possesses a crucial lysine residue at the trypsin reactive site. These inhibitors have molecular masses of 8.5 kDa and isoelectric points of 4.6-5.6. They exist mainly as dimers under physiological conditions. Amino acid analysis revealed high levels of half-cystine, serine, aspartate and proline but low levels of methionine and aromatic amino acids. Amino-terminal sequence analysis revealed that each of the 4 isoinhibitors has a conserved core sequence but all are divergent at the N-terminal end. These inhibitors belong to the Bowman-Birk (BBI) family of proteinase inhibitors as reflected by their inhibitory properties, amino acid composition and homology to other BBI.

Item Type: Article
Uncontrolled Keywords: ENZYME-INHIBITORS; LEGUMES-; HORSE-GRAM; PROTEINASES-INHIBITORS
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
600 Technology > 08 Food technology > 22 Legumes-Pulses
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 09 Aug 2008 05:15
Last Modified: 01 Jul 2015 11:43
URI: http://ir.cftri.com/id/eprint/7786

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