Abstract
Sedimentation and diffusion measurements were made in concn. range 0.17-0.8 g/100 ml on human serum albumins obtained by ethanol fractionation and by electrophoretic separation. Effect of variation in composition of the buffer was examined with the result that, for a given prepn., sedimentation or diffusion may be affected at finite concns., but values extrapolated to zero concn. do not differ significantly. Values of [image] and [image] very slightly from one prepn. to another, indicating'' difference''s in avg. molecular wt. Evidence presented suggests that this is due to separation of groups of molecules of different molecular characteristics rather than to irreversible changes produced by buffer conditions. The faster of the 2 components which appear on electrophoresis of albumin at pH 4.0 was isolated. Its sedimentation and diffusion properties were indistinguishable from those of whole albumin.
Keywords