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Partial characterization of the lysine rich 280KD globulin from common buckwheat (Fagopyrum esculentum Moench): Its antigenic homology with seed proteins of some other crops
Author(s) -
Rout M. K.,
Chrungoo N. K.
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201173
Subject(s) - fagopyrum , legumin , amaranth , globulin , storage protein , biology , molecular mass , glutelin , lysine , botany , biochemistry , amino acid , gene , enzyme , immunology
A high molecular weight (HMW) globulin, the main storage protein in grains of the common buckwheat (Fagopyrum esculentum Moench) has been partially characterized. The protein exists as an oligomeric complex with molecular mass of 280 kD and is composed of three groups (α, β and γ of polypeptides with molecular weights ranging between 55‐60, 32‐44 and 16‐29 kD respectively. The protein showed serological cross reactivity with globulins of soya bean, mung bean and pea. Antibodies raised against the purified protein did not recognize the storage proteins from broad bean, rice, wheat and grain amaranth. The 280 kD globulin of buckwheat grains belongs to the legumin family of proteins.