"Substrate Inhibition" of Intestinal Glycosidases.
- 1 January 1960
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 14 (8) , 1797-1808
- https://doi.org/10.3891/acta.chem.scand.14-1797
Abstract
The influence of substrate concentration on the initial rate of hydrolysis of different glycosides by hog intestinal glycosidases has been studied. In some cases marked ''substrate inhibition'' was observed at 0.139 M substrate concentration, which is the concentration previously used as a standard concentration for the determination of intestinal glycosidase activities. Transglycosylation plays an important role in the ''substrate inhibition'' but it is not the only factor involved. The use of 0.028 M substrate concentration as a standard concentration for the determination of intestinal glycosidase activities, rather than 0.139 M, is recommended. The influence of this lower substrate concentration on the absolute and relative activities of some purified hog intestinal glycosidases, and of crude hog intestinal glycosidase preparations, on different substrates has been determined. Methods for determination of intestinal glycosidase activities are described, and units for expressing intestinal glycosidase activities are defined.This publication has 5 references indexed in Scilit:
- Characterization of Hog Intestinal Trehalase.Acta Chemica Scandinavica, 1960
- Hog Intestinal Isomaltase Activity.Acta Chemica Scandinavica, 1960
- The determination of enzyme inhibitor constantsBiochemical Journal, 1953
- Über die Reduktion der 3,5‐Dinitrosalicylsäure durch ZuckerHelvetica Chimica Acta, 1951
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934