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Seed protein characterisation and nitrogen fixation rates in the chickpea mutant hyprosola and its parent
Author(s) -
Schroeder Hartmut E,
Gibson Alan H,
Oram Rex N,
Shaikh M Anwarul Quader
Publication year - 1988
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740440105
Subject(s) - globulin , mutant , albumin , amino acid , biochemistry , cultivar , biology , chemistry , food science , botany , gene , endocrinology
The amino acid composition of the seed proteins of Hyprosola, a high protein, high yielding mutant of chickpea (Cicer arietinum L), differed little from that of its parental cultivar, Faridpur‐1. Oser's essential amino acid index was 76‐5 in the mutant and 76‐7 in the parent. Hyprosola seed has higher crude protein, extractable protein, globulin and albumin contents than Faridpur‐1. The mutant had an albumin/globulin ratio of 0‐23 compared with the parental value of 0‐21. The mutant oligomeric proteins differed quantitatively and qualitatively from the parent on cellulose acetate electrophoretograms. The polypeptide composition of globulins and albumins fractionated by SDS‐PAGE differed markedly in the intensity of many bands but not in the mobility of any polypeptides. Nitrogen fixation (acetylene reduction) rates were similar in the two cultivars, and in both hydrogen evolution utilised 45 % of the electron flow through nitrogenase.