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The purification and partial amino acid sequence of a polypeptide from the glutelin fraction of rice grains; homology to pea legumin
Author(s) -
Zhao Wen-Ming,
Gatehouse John A.,
Boulter Donald
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)81056-4
Subject(s) - glutelin , legumin , storage protein , protein subunit , biochemistry , chemistry , chromatography , amino acid , globulin , urea , biology , gene , immunology
The glutelin fraction was extracted from grain meals of rice ( Oryzea sativa ) with 50 mM Tris‐HCl buffer (pH 8.8) containing 6 M urea and 10 mM 2‐mercaptoethanol. Polypeptides of glutelin were separated and purified by ion‐exchange chromatography under denaturing conditions. Analysis by two‐dimensional gel electrophoresis showed that 2 major polypeptides of the rice glutelin fraction, M r 36 000 and 22 000, were linked in disulphide bonded pairs containing one M r 36 000 and one M r 22 000 subunit. A partial amino acid sequence of the purified M r 22 000 glutelin subunit showed it to be homologous to the β‐subunit of pea legumin, a storage protein which also contains disulphide‐linked subunit pairs ( M r 38 000 and M r 22 000). It is therefore proposed that the major component of rice glutelin is a legumin‐like protein.