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

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.

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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 .

Item Type: Article
Uncontrolled Keywords: beta-globulin; binding; kinetics; MIHP; polymer; protein-ligand interaction
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
600 Technology > 08 Food technology > 19 Lipids-oils/fats > 01 Oilseeds
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 12 Mar 2018 06:45
Last Modified: 12 Mar 2018 06:45
URI: http://ir.cftri.com/id/eprint/4488

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