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Interaction of myo inositol hexaphosphate (MIHP) with Beta globulin from Sesamum indicum (L.).

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Title Interaction of myo inositol hexaphosphate (MIHP) with Beta globulin from Sesamum indicum (L.).
 
Creator Rajendran, S.
Prakash, V.
 
Subject 03 Proteins
01 Oilseeds
 
Description fl-Globulin, the low molecular weight protein fraction from Sesamum indicum L., interacts with myo-inositol
hexaphosphate (MIHP) maximally at pH 3.0, with concomitant precipitation up to 85 2 2% at an MIHP
concentration of 8 x 10 - M. The kinetics of interaction as followed by stopped-flow spectrophotometry
suggested the reaction to be of pseudo first-order, having an initial fast step followed by a relatively slow step
of rate constants 1 . 9 ~ s - * , r espectively at 1 x 1 0 - 4 M~ I HP concentration. The
analysis of the complex indicated the presence of polymer as seen in sedimentation velocity experiment. This
was accompanied by conformational change of a three-fold decrease in fl-structure and also an increase in
fluorescence emission intensity accompanied with a red shift from 330 to 334 nm. Stoichiometric analysis of
MIHP binding suggested four independent binding sites for MIHP, with a free energy change, AGO = -5.1 kcal
mol- resulting from a binding constant of 3.6 x lo3 M - I .
 
Date 1993
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/4488/1/Int.%20J.%20Peptide%20Protein%20Res.%2042%2C%201993.%2078-83.pdf
Rajendran, S. and Prakash, V. (1993) Interaction of myo inositol hexaphosphate (MIHP) with Beta globulin from Sesamum indicum (L.). International Journal of Peptide and Protein Research, 42 (1). pp. 70-83.