Esterification of J chain and its effect on electrophoretic mobility in sodium dodecyl sulfate polyacrylamide gels.
Sodium dodecyl sulfate polyacrylamide gel electrophoresis yields mobilities indicative of molecular weights of approximately 27 000 for human J chain and approximately 14 000 for nurse shark J chain, in contrast to values of approximately 15 500 and approximately 12 200, respectively, obtained by other methods. The relatively high content of acidic amino acids of human J chain as compared to nurse shark J chain suggested that the greater error in the sodium dodecyl sulfate determined molecular weight for human J chain may be due to a charge anomaly. The overall net negative charge on human J chain was decreased by forming methyl esters of the carboxyl groups, resulting in a sodium dodecyl sulfate determined molecular weight of approximately 17 700. Methylated nurse shark J chain did not show a significant difference in sodium dodecyl sulfate electrophoretic mobility from the non-methylated form. These results form the basis for a possible explanation of an occasional artifact in a widely used analytical method.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D004952:Esters; D007144:Immunoglobulin J-Chains; D007075:Immunoglobulin M; D008970:Molecular Weight; D012754:Sharks; D012967:Sodium Dodecyl Sulfate; D014508:Urea
D004952:Esters; D007144:Immunoglobulin J-Chains; D007075:Immunoglobulin M; D012967:Sodium Dodecyl Sulfate; D014508:Urea