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Kinetic and structural studies on the interaction of proteinase inhibitor from Bolichos biflorus horsegram.

Ramasarma, P. R. and Appu Rao, A. G. and Rajagopal Rao, D. (1994) Kinetic and structural studies on the interaction of proteinase inhibitor from Bolichos biflorus horsegram. Journal of Agricultural and Food Chemistry, 42 (10). pp. 2139-2146.

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Abstract

One of the major components of multiple inhibitors from Dolichos biflorus (horse gram) (HGPI) inhibits both bovine trypsin and chymotrypsin, resembling other Bowman-Birk-type protease inhibitors. Ultraviolet absorbance measurements indicate the presence of two tyrosine residues, the absence of tryptophan, and the dominance of disulfide linkages in the molecule. The intrinsic fluorescence emission maximum (Amax 336 nm) is due to the tyrosine residues in the hydrophilic environment. Disulfide linkages and tyrosine residues contribute to the near-ultraviolet circular dichroism spectra. Far-ultraviolet circular dichroism measurements indicate the absence of any helical structure, 31% 13 structure, and the rest aperiodic structure. Aromatic amino acids are involved in the interaction of the inhibitor with trypsin or chymotrypsin. The equilibrium constants for the interaction of HGPI with chymotrypsin/trypsin were 2.9 x 105 and 5.2 x 105 M-1, respectively, with an estimated stoichiometry of 1:1 with either of the enzymes.

Item Type: Article
Uncontrolled Keywords: Proteinase inhibitors; conformation; association with trypsin and chymotrypsin; circular dichroism measurements
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
600 Technology > 08 Food technology > 22 Legumes-Pulses
Divisions: Dept. of Biochemistry
Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 08 May 2012 10:43
Last Modified: 08 May 2012 10:43
URI: http://ir.cftri.com/id/eprint/4531

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