The 12 S globulin of rapeseed represents an oligomeric protein with a molecular weight of 300,000. It is composed of 6 subunits, which are arranged in a trigonal. antiprism with the point group symmetry 32 (D3).Each subunit contains smaller units (polypeptide chains) with molecular weights in the range of 18,500 to 31,000. The protein contains the following 4 polypeptide chains differing by their molecular weights in the SDS-electrophoresis: 18,500 k 800, 21,100 500, 26,800 900, 31,200 k 1,600.According to its quaternary structure the protein dissociates under milieu conditions : low ionic strength extremely high or low pHThe secondary structure of the protein is characterized by a low (1 1 yo) content of a-helix and a relatively high (31 %) content of &conformation.11/12 S globulins in the seeds of different plant species and botanical families.Owing to its structure and physico-chemical properties the rapeseed protein is closely related to otherThe 12 S globulin represents a main storage protein in the seeds of Brassica species [I -61.
21-33% of the nitrogen in sodium chloride extracts of defatted rapeseed varieties or 18-28The globulin was first isolated by BHATTY et al.[I] from oil-free rapeseed meal by extraction with 10 % sodium chloride, precipitation by dialysis against water, and chromatographic separation on Sephadex G-100. SIMARD et al. 191 used the technique of fractionating precipitation and dissolution by ammonium sulphate for the isolation of the protein. SCHWENKE et al. [lo] described a combined gel and ionic-exchange chromatographic purification of the 12 S globulin. The present paper summarizes the results of research on the physico-chemical properties and structure of the 12 S globulin of rapeseed. of the total seed nitrogen correspond to this protein [l, 7, 81.
Hydrodynamic properties and molecular weightAfter isolation and purification of the protein BHATTY et al.[l] could show by ultracentrifugal analysis that this rapeseed globulin, owing to its sedimentation property, corresponds to the group of 11/12 S seed proteins. The authors found a sedimentation coeffi-