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The inhibition of erythrocyte glyceraldehyde-3-phosphate dehydrogenase. In situ PMR studies.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 1984 Jun 19; Vol. 804 (2), pp. 209-15. - Publication Year :
- 1984
-
Abstract
- The kinetics of inhibition of human erythrocyte glyceraldehyde-3-phosphate dehydrogenase by iodoacetate were studied in the intact cell and in vitro. The kinetics were determined using 1H-NMR to follow solvent exchange of 1H and 2H at the C-2 position of lactate. The exchange occurs via a series of enzyme-catalysed reactions, including that catalysed by glyceraldehyde-3-phosphate dehydrogenase. A direct assay with quenching of the inhibition was also used to check the results. Iodoacetate was shown to act as an active site-directed inhibitor of the dehydrogenase. The enzyme inhibition patterns, which are characterised by a binding step and a kinetic step, are similar in situ and in vitro. Membrane binding, however, was found to alter the inhibition pattern for the enzyme in vitro.
- Subjects :
- Deuterium
Glyceraldehyde-3-Phosphate Dehydrogenases antagonists & inhibitors
Humans
In Vitro Techniques
Iodoacetic Acid
Kinetics
Magnetic Resonance Spectroscopy methods
Protein Binding
Radioisotope Dilution Technique
Erythrocytes enzymology
Glyceraldehyde-3-Phosphate Dehydrogenases blood
Iodoacetates pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 804
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 6372868
- Full Text :
- https://doi.org/10.1016/0167-4889(84)90151-4