Abstract

The activities of alkaline phosphatase (ALP) from plasma at several ages were determined, and the origin of plasma ALP was investigated on the basis of the electrophoretic migration and the optimum pH in IS strain of rats (IS rats) and SD strain of rats (SD rats). Both in IS and SD rats, the activity was highest at the youngest group (8 weeks), and it decreased rapidly with age. The activities in IS rats at 8 and 10 weeks of age were 63% and 66% of those in SD rats. At 20 and 30 weeks of age, the difference was not clear. The zymogram gave two bands for SD rat plasma. One of the bands was regarded as the intestinal isozyme and the other was the osseous and/or the hepatic isozymes. The zymograms of IS rat plasma gave only one band which fairly consistent with that of the osseous or hepatic isozyme, and no intestinal isozyme was detected. The mobility of the intestinal isozyme was not completely identical between IS and SD rats. Thus, the molecular difference in the intestinal isozyme was thought to be a cause of the difference in the ALP activity and isozyme composition of the plasma between these two strains. The zymograms for other tissues did not show any difference between IS and SD rats. The effect of the change in pH on ALP activity also suggested that the plasma ALP in IS rats did not contain any intestinal isozyme.

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