Abstract
Summary
Alkaline phosphatase activity was measured in hormonally stimulated pancreatic juice from six dogs and in pancreatic fistula fluid from a human subject. Isoenzyme characterization studies, based on different susceptibilities to urea and l-phenylalanine inhibition and to heat inactivation indicated similarities between canine and human pancreatic secretory alkaline phosphatase. Compared to intestinal alkaline phosphatase, the pancreatic isoenzyme was much more sensitive to heat inactivation and urea inhibition but much more resistant to l-phenylalanine inhibition. The electrophoretic mobility of the enzyme present in human pancreatic juice was different from that of human hepatic, bone, or intestinal alkaline phosphatase.
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