Hydrodynamic and quasi-elastic light scattering studies on the 12S globulin from rapeseed.

The 12S globulin, one of the major storage proteins of rapeseeds, has the following physico-chemical constants, as determined by ultracentrifugation, quasi-elastic light scattering measurements and gel chromatography: sedimentation coefficient S20(0), w = 12.7 x 10(-13) s; diffusion coefficient (quasi-elastic light scattering) D20(0), w = 3.8 x 10(-7) cm2 S-1; Stokes radius (by quasi-elastic light scattering) Rs = 5.7 nm and (by gel chromatography) Rs = 5.5 nm; partial specific volume (calculated from the amino acid composition) v(-) = 0.729 ml g-1; molecular weight Ms, D = 300,000 daltons, Ms, Rs = 294,000 daltons (Rs from the gel chromatography); frictional ratio f/fo = 1.28.