Clinical Chemistry
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Clinical Chemistry 41: 435-438, 1995;
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Clinical Chemistry, Vol 41, 435-438, Copyright © 1995 by American Association for Clinical Chemistry

Determination of alpha-amylase activity: methods comparison and commutability study of several control materials

G Gubern, F Canalias and FJ Gella
Departament de Bioquimica i Biologia Molecular, Universitat Autonoma de Barcelona, Spain.

Six different methods for alpha-amylase determination were compared by assaying human serum samples covering a wide range of alpha-amylase values. All the methods studied use as substrate a maltooligosaccharide with a chromophore group at the reducing end; some are chemically blocked at the nonreducing end. Intermethod comparison by regression and correspondence analyses showed significant differences for two methods. The commutability of 12 commercial control materials containing alpha-amylase was also assessed by the different methods in comparison with human serum specimens containing the pancreatic and salivary isoenzymes. We also studied the behavior of pancreatic and salivary materials prepared in our laboratory. Control materials with alpha-amylase of non-human origin were not commutable with the enzyme in human sera and should not be used for intermethod calibration.


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A. Mosca, R. Paleari, A. Made, C. Ferrero, M. Locatelli, and F. Ceriotti
Commutability of control materials in glycohemoglobin determinations
Clin. Chem., March 1, 1998; 44(3): 632 - 638.
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Copyright © 1995 by the American Association for Clinical Chemistry.