Electrophoretic polymorphism of human C4 is due to charge differences in the alpha chain, presumably in the C4d fragment.
Various common C4 gene products were isolated from serum by immunoprecipitation. After reduction the C4 alpha-, beta-, and gamma-polypeptide chains were studied by two-dimensional electrophoresis. Isoelectrofocusing was performed in the first dimension and sodium dodecyl sulphate polyacrylamide gradient gel electrophoresis in the second. The charge differences behind the electrophoretic C4 polymorphism were shown to reside in the 95,000-u (atomic mass units) alpha-chain. Charge variation closely mirroring the alpha-chain differences were also found in a 49,000-u fragment of the alpha-chain, most probably C4d. The basic beta-chain could not be studied in detail, but no differences were observed with regard to molecular weight or charge of the gamma-chains of the different C4 gene products.
D003181:Complement C4 / Q000235:genetics* / Q000302:isolation & purification; D004586:Electrophoresis; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007525:Isoelectric Focusing; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D011110:Polymorphism, Genetic
D003181:Complement C4; D010446:Peptide Fragments