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Dissociation, aggregation of sesame L- globulin in nonionic detergent solution.

Lakshmi, T. S. and Nandi, P. K. (1978) Dissociation, aggregation of sesame L- globulin in nonionic detergent solution. International Journal of Peptide and Protein Research, 12. pp. 197-203.

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Abstract

Nonionic detergents Triton X-l00 and Brij 36T induce dissociation and aggregation of the protein sesame Q-globulin above the critical micelle concentrations (crnc) of the detergents. Spectrophotometric titration in Triton shows no change in the pK1nl value of tile tyrosyl groups at 1 X 10-3 M detergent where both dissociation and aggregation of the protein are observed. Fluorescence measurement does not indicate any change in the environment of the tryptophan groups of the protein in Brij. Viscosity measurements show no major conformational change of the protein in the detergent solution. Binding measurements suggest that perhaps micelles of the detergent predominantly bind to the protein. The detergent micelles preferentially bind to the exposed hydrophobic surfaces of the protein subunits. The association of the protein detergent complex through electrostatic interaction is probably responsible for the formation of the aggregates.

Item Type: Article
Uncontrolled Keywords: binding induced dissociation of protein; binding of nonionic detergent to protein; dissociation, aggregation of protein; protein-nonionic detergent interaction; sesame protein-nonionic detergent interaction
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
600 Technology > 08 Food technology > 19 Lipids-oils/fats > 01 Oilseeds
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 28 Dec 2016 07:54
Last Modified: 28 Dec 2016 07:54
URI: http://ir.cftri.com/id/eprint/3800

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