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Clinical Chemistry 26: 846-853, 1980;
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Clinical Chemistry, Vol 26, 846-853, Copyright © 1980 by American Association for Clinical Chemistry

Recent advances in measurement of amylase activity--a comparative study

RA Kaufman and NW Tietz

We evaluated four kinetic amylase procedures with respect to kinetics, analytical range, blank rates, reagent stability, reagent impurities, interfering substances, and intrinsic sensitivities. Each of the methods is shown to have its own unique advantages and disadvantages. A preliminary discussion of some alternative methods, in which glycosidic p-nitrophenyl alpha-oligosaccharides are substrates, is included.


The following articles in journals at HighWire Press have cited this article:


Home page
 Protein Eng Des SelHome page
M. H. Rivera, A. Lopez-Munguia, X. Soberon, and G. Saab-Rincon
{alpha}-Amylase from Bacillus licheniformis mutants near to the catalytic site: effects on hydrolytic and transglycosylation activity
Protein Eng. Des. Sel., July 1, 2003; 16(7): 505 - 514.
[Abstract] [Full Text] [PDF]


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