Affinity electrophoresis of alkaline phosphatase using polyacrylamide gels

Abstract

A method is described for the separation of liver and bone isoenzymes of alkaline phosphatase in serum using wheat germ lectin affinity electrophoresis in a polyacrylamide gel matrix. The electrophoretic mobilities of liver and intestinal isoenzyme are essentially not affected by lectin, but the bone enzyme is retarded and separated from the liver fraction. Affinity electrophoresis in polyacrylamide gel, combined with agarose gel electrophoresis, and a solid-phase linked antibody precipitation procedure for intestinal alkaline phosphatase allowed the various isoenzyme fractions, biliary, liver, bone and intestinal, to be quantitated.