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Denaturation of the high molecular weight protein fraction of mustard (Brassica juncea), and rapeseed (Brassica compestris) by urea or guanidinium hydrochloride.

Gururaj Rao, A. and Narasinga Rao, M. S. (1983) Denaturation of the high molecular weight protein fraction of mustard (Brassica juncea), and rapeseed (Brassica compestris) by urea or guanidinium hydrochloride. Journal of Biosciences, 5. pp. 311-320.

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Abstract

Urea and guanidinium hydrochlOride dissociate the 12S protein of mustard and rapeseed to 1.8 S protein and the extent of dissociation depends on the concentration of the denaturant. Mustard (Bras$imjuncea) protein is more readily dissociated than the rapeseed (Bras$im rompestrU) protein. The reagents denature the protein as evidenced by increase in viscosity, appearance of difference spectra and quenching of fluorescence. Rapeseed protein is denatured more readily than the mustard protein. Analysis of viscosity, spectral and fluorescence data suggests that the first event in the denaturation reaction is the perturbation of the aromatic amino acid residues followed by their exposure to the solvent medium and unfolding of the protein molecule.

Item Type: Article
Uncontrolled Keywords: Mustard protem; rapeseed protein; denaturation; urea; guanidinium hydrochloride.
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
600 Technology > 08 Food technology > 19 Lipids-oils/fats > 06 Rapeseed
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 12 Dec 2016 11:34
Last Modified: 12 Dec 2016 11:34
URI: http://ir.cftri.com/id/eprint/3694

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