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Characterization of the 12S storage protein of Brassica napus (cruciferin): Disulfide bonding between subunits
Author(s) -
Rödin Joakim,
Rask Lars
Publication year - 1990
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1990.tb02097.x
Subject(s) - protein subunit , brassica , disulfide bond , rapeseed , storage protein , chemistry , immunoglobulin light chain , biochemistry , electrophoresis , gel electrophoresis , biology , genetics , botany , gene , food science , antibody
Cruciferin (12S globulin) is a large, neutral, oligomeric protein synthesized in rapeseed ( Brassica napus ) during the seed development. It is composed of six subunit pairs. Each pair consists of one heavy α chain (30 kDa) and one light β chain (20 kDa). Four different subunit pairs exist. In contrast to earlier studies, our investigations using two‐dimensional electrophoresis showed, that the majority of α and β chains of each subunit are disulfide‐linked. Analysis of subunit composition of cruciferin hexamers by ion‐exchange chromatography suggested that a large array of hexamers exist, composed of mixed combinations of the four subunits.