Proteins of Italian millet: amino acid composition, solubility fractionation and electrophoresis of protein fractions

Monteiro, P.V. and Virupaksha, T.K. and Rao, D.R. (1982) Proteins of Italian millet: amino acid composition, solubility fractionation and electrophoresis of protein fractions. Journal of the Science of Food and Agriculture, 33 (11). pp. 1072-1079.

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Abstract

Determination of the protein contents of 14 Setaria italica cv. revealed considerable cv. differences. The total protein of the 14 cv. was fractionated into albumin-globulin, prolamin and glutelin fractions. The prolamin fraction constituted the major storage protein of the grain. There was a positive correlation between protein and prolamin contents of the seeds and the increase in protein content was largely due to an increase in the prolamin content. The amino acid composition of each of the 14 cv. and the individual protein fractions from 3 cv. were determined. The limiting amino acids were lysine followed by tryptophan, methionine and cystine. The lysine content of the grain decreased with increase in protein content. The total protein had a rather high leucine content. SDS-polyacrylamide gel electrophoresis of the protein fractions indicated similarities in the prolamin fraction and differences in the albumin-globulin and glutelin fractions of the different cv

Item Type: Article
Author Affiliation: Cent. Food Technol. Res. Inst., Mysore 570 013, Karnataka, India.
Subjects: Plant Protection
Plant Physiology and Biochemistry > Biochemistry
Divisions: Millet
Depositing User: Mr B Krishnamurthy
Date Deposited: 06 Aug 2012 03:55
Last Modified: 06 Aug 2012 03:55
Official URL: http://dx.doi.org/10.1002/jsfa.2740331104
URI: http://eprints.icrisat.ac.in/id/eprint/7131

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