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

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Title Kinetic and structural studies on the interaction of proteinase inhibitor from Bolichos biflorus horsegram.
 
Creator Ramasarma, P. R.
Appu Rao, A. G.
Rajagopal Rao, D.
 
Subject 29 Protein Chemistry
22 Legumes-Pulses
 
Description 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.
 
Date 1994
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://ir.cftri.com/4531/1/Journal_of_Agricultural_and_Food_Chemistry_1994_42_2139-2146.pdf
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.