Diffusion-dependent rates for the hydrolysis reaction catalyzed by glyoxalase II from rat erythrocytes
- 1 November 1988
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 27 (24) , 8818-8822
- https://doi.org/10.1021/bi00424a020
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 14 references indexed in Scilit:
- Molecular cloning of the Pseudomonasputida glyoxalase I gene in EscherichiacoliBiochemical and Biophysical Research Communications, 1987
- Fractional diffusion-limited component of reactions catalyzed by acetylcholinesteraseBiochemistry, 1986
- Diffusion-limited component of reactions catalyzed by Bacillus cereus .beta.-lactamase IBiochemistry, 1984
- Nonstereospecific substrate utilization in the glyoxalase I reactionBiochemistry, 1983
- Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variationBiochemistry, 1982
- Acetylcholinesterase: evidence that sodium ion binding at the anionic site causes inhibition of the second-order hydrolysis of acetylcholine and a decrease of its pKα as well as of deacetylationBiochemical Journal, 1981
- Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligandsBiochemistry, 1980
- Purification of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from rat erythrocytesAnalytical Biochemistry, 1979
- Evolution of enzyme function and the development of catalytic efficiencyBiochemistry, 1976
- GLUTATHIONE THIOLESTERASE1954