HYDRODYNAMIC AND QUASI‐ELASTIC LIGHT SCATTERING STUDIES ON THE 12S GLOBULIN FROM RAPESEED*

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Abstract
The 12S globulin, one of the major storage proteins of rapeseeds, has the following physico-chemical constants, as determned by ultracentrifugation, quasi-elastic light scattering measurements and gel chromatography: sedimentation coefficient .**GRAPHIC**. = 12.7 .times. 10-13 s; diffusion coefficient (quasi-elastic light scattering) .**GRAPHIC**. = 3.8 .times. 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) .hivin.v = 0.729 ml g-1; molecular weight Ms, D = 300,000 daltons, Ms Rs = 294,000 daltons (Rs from the gel chromatography); and frictional ratio f/fo = 1.28.