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Clinical Chemistry 28: 2201-2205, 1982;
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Clinical Chemistry, Vol 28, 2201-2205, Copyright © 1982 by American Association for Clinical Chemistry

Mechanism of action of human pancreatic and salivary alpha-amylase on alpha-4-nitrophenyl maltoheptaoside substrate

EO Hagele, E Schaich, E Rauscher, P Lehmann, H Burk and AW Wahlefeld

We evaluated the enzymic mechanism by which alpha-4-nitrophenyl maltoheptaoside serves as a substrate for serum amylase (EC 3.2.1.1). Because polymeric substrates possess many potential sites of cleavage, the expression of enzymic activity as the number of micromoles of substrate transformed under defined conditions by an enzyme must be changed to "one microequivalent of group transformed." Therefore, we measured the activity of the isoenzymes of alpha-amylase with regard to suitable oligosaccharide substrates, which allowed us to express the catalytic activity in IUB units (U). By "high-performance" liquid chromatography we investigated the mechanism of human pancreatic and salivary alpha-amylase action, both alone and in combination with alpha- glucosidase (EC 3.2.1.20). On the basis of these results, we can describe exactly the entire reaction sequence and determine the stoichiometric coefficient of 4-nitrophenol within 0.02 mol/L (SD) produced under the assay conditions.


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


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 Exp PhysiolHome page
H. Cevik Aras and J. Ekstrom
Pentagastrin-induced nitric oxide-dependent protein secretion from the parotid gland of the anaesthetized rat
Exp Physiol, November 1, 2006; 91(6): 977 - 982.
[Abstract] [Full Text] [PDF]


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Copyright © 1982 by the American Association for Clinical Chemistry.