Rapid electrophoretic analysis of heterogeneity of bovine serum albumin using a linear polyacrylamide-coated capillary.

Bovine serum albumin was separated into three major peaks and two or three minor peaks at pH 7.4 within 12 min by capillary zone electrophoresis using a linear polyacrylamide-coated capillary. The two major peaks, having medium and low mobilities, were assigned to the monomers of nonmercaptoalbumin and mercaptoalbumin, respectively. On the other hand, cross-linked albumins were distributed as a broad peak around the major peak with high mobility. Thus, commercially available bovine serum albumins from various sources were revealed to have a wide variety of heterogeneity in terms of their respective components.