Studies on serum amylase in normal man and in acute pancreatitis
MacGregor, I.L.; Zakim, D.
Australian and New Zealand Journal of Medicine 6(6): 551-556
1976
ISSN/ISBN: 0004-8291 PMID: 1071539 Document Number: 107382
Amylase isoenzymes in serum, urine, saliva, jejunal juice and pancreatic tissue were separated by isoelectric focusing. The isoamylase patterns indicated that most of the amylase activity in normal serum is of salivary gland origin. Pancreatic amylase is characteristically predominant in acute pancreatitis. The increased renal clearance of amylase in acute pancreatitis may be partly due to the increased proportion of the smaller molecular weight pancreatic amylase, but a demonstrated increase in the renal clearance of salivary amylase in acute pancreatitis suggests a renal cause also. Autopsy pancreas samples devoid of TAME (p-tosyl arginine methyl ester) esterase activity, e.g., trypsin and plasma enzymes such as thrombin and plasmin, had isoenzyme patterns which were different from those with free proteolytic activity. Incubation of TAME esterase free pancreas with trypsin converted the former isoamylase pattern to one with the predominant isoenzymes focusing coincident with the predominant peak in serum from acute pancreatitis, jejunal aspirate and TAME esterase positive autopsy pancreas. Such conversion suggests that pancreatic amylase is synthesized in a form different from that found in the intestinal lumen and serum.