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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.
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Kaufman et al. (1980) studied this question.
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