Electrophoretic studies on alkaline phosphatases in normal and zinc intoxicated rats.

Polyacrylamide gel electrophoresis was used to characterize the isoenzymes of serum alkaline phosphatase in the rat. The electrophoresis of serum from normal rats resulted in two bands of alkaline phosphatase activity. A prominent band in serum corresponded in electrophoretic mobility to the alkaline phosphatase from bone and intestinal tissue extracts and also a slower migrating liver isoenzyme. A less prominent, fast migrating band in serum had a mobility similar to a faster migrating liver tissue extract isoenzyme. This band only represented 1-2% of the total alkaline phosphatase present in the serum of normal rats but approximately 15% of the total alkaline phosphatase in the serum of rats fed excess levels of zinc. The study also revealed an alteration in the electrophoretic mobility of alkaline phosphatase in bone homogenate by the addition of deactivated serum to the homogenate. The addition of deactivated serum did not alter the electrophoretic mobility of the liver and intestinal alkaline phosphatases in rats.