RAPID MEASUREMENT OF SERUM PANCREATIC AMYLASE

A simple, rapid assay for the pancreatic isoenzyme of human serum amyl ase was developed. The assay utilized an immunoabsorbent prepared by c oating latex beads with a monoclonal antibody specific for pancreatic amylase. Treatment of patient serum with immunoabsorbent removed pancr eatic amylase, and measurement of residual amylase activity with stand ard total amylase methodology allowed estimation of the pancreatic amy lase content. Extraction efficiency of pancreatic amylase was consiste nt at amylase concentrations up to 1,000 U/L (y = 0.97 x + 16.7 U/L; r = 0.9995). The assay was standardized with purified pancreatic amylas e added to neonatal serum (low endogenous activity). A comparison of p atient specimen results with the results of a standard technique (cell ulose acetate electrophoresis) yielded an excellent correlation (immun o-absorption result = 0.96 electrophoresis result + 1.2 U/L; r = 0.987 ). Salivary amylase did not interfere with the assay until levels exce eded 1,000 U/L. Daily analysis of a frozen serum pool yielded a coeffi cient of variation of 9.2% at mean pancreatic amylase value of 54 U/L (+/- 5 U/L). A normal range study found a strong influence of age, wit h pancreatic amylase levels increasing dramatically in the first 3 yea rs of life, to stabilize at a range of 0-66 U/L thereafter. (C) 1994 W iley-Liss, Inc.