Separation of components of human globulins by capillary zone electrophoresis using a linear polyacrylamide-coated...

Eleven commercially available protein preparation from human serum were subjected to capillary zone electrophoresis (CZE) using a linear polyacrylamide-coated capillary at pH 7.4. Transferrin, complement C3 and C-reactive protein were each separated into one major peak and several minor peaks. alpha 1-Antitrypsin was separated into two major peaks and three minor peaks. alpha 2-HS-glycoprotein showed four major peaks with a leading shoulder. Haptoglobin, alpha 2-macroglobulin, alpha 1-acid-glycoprotein and prealbumin were detected as relatively wide peaks. Ceruloplasmin showed one major peak with notches, and two minor and several notched peaks. Only low density lipoprotein showed no peaks. A mixture of five of the protein preparations was separated into individual components, as well as individual isoforms. When the same mixture was analyzed by CZE using an uncoated capillary, a much poorer resolution was obtained. Application of this CZE system to albumin-depleted serum demonstrated that it is very useful for analyzing globulin components in serum.