On the heterogeneity of serum albumin: effect of sodium dodecyl sulphate on agarose chromatography of the protein.

The chromatographic behaviour of serum albumin changes if it is dissolved in an aqueous solution of sodium dodecyl sulphate (SDS) and is left at room temperature or is heated. Instead of emerging as one peak from an agarose column it emerges as more than one peak and the protein in each when rechromatographed elutes in more than one peak. Electropherograms made in the presence of SDS of the protein in these peaks show multiple banding from proteins migrating with a wide range of molecular weights. The chromatographic and electrophoretic behaviour of serum albumin in the presence of SDS suggests that the protein is not a simple monomer and alternative explanations for this behaviour are discussed.