Clinical Chemistry
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Clinical Chemistry 34: 2552-2555, 1988;
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Clinical Chemistry, Vol 34, 2552-2555, Copyright © 1988 by American Association for Clinical Chemistry

Assay of pancreatic amylase with use of monoclonal antibodies evaluated

M Zaninotto, R Bertorelle, S Secchiero, M Plebani and A Burlina
Cattedra di Chimica e Microscopia Clinica, Universita degli Studi di Padova, Ospedale Civile, Italy.

To evaluate a new method for measuring pancreatic amylase in serum, in which the salivary isoenzyme is inhibited with a specific monoclonal antibody, we determined the activity of pancreatic and salivary amylase in sera from 103 healthy subjects and from 114 hospitalized patients having a wide range of total amylase activities. CVs for the proposed method ranged from 0.8% to 5.1% (within day) and from 2.3% to 6.6% (day to day). Results correlated well with those obtained by the wheat-germ inhibition method (r = 0.998) and by electrophoresis on cellulose acetate. Analytical-recovery studies confirmed the good specificity of the monoclonal antibody for salivary amylase (97%) and its low cross- reactivity (0.6%) toward pancreatic amylase. The assay procedure presents a wide range of linearity (141-1817 U/L) and can easily be adapted to an automated kinetic system. We found the proposed method suitable for routine determinations of pancreatic amylase.


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Y. Morishita, Y. Iinuma, N. Nakashima, K. Majima, K. Mizuguchi, and Y. Kawamura
Total and Pancreatic Amylase Measured with 2-Chloro-4-nitrophenyl-4-O-{beta}-D-galactopyranosylmaltoside
Clin. Chem., July 1, 2000; 46(7): 928 - 933.
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