Physiological Concentrations of Lactate Dehydrogenases and Substrate Inhibition

Lactate dehydrogenases at physiological concentrations are inhibited by high concentrations of pyruvate when the enzyme and the pyruvate are incubated in the presence of oxidized nicotinamide-adenine dinucleotide before assay. The inhibition is much more pronounced with the H-type than with the M-ty...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1970-06, Vol.168 (3936), p.1236-1238
Main Authors: Everse, Johannes, Berger, Robert L., Kaplan, Nathan O.
Format: Article
Language:English
Subjects:
Animals
Chickens
Coenzymes
Dehydrogenases
Enzyme substrates
Enzymes
Isoenzymes
L-Lactate Dehydrogenase - antagonists & inhibitors
Lactates
Methods
NAD - pharmacology
Oxidation
Pyruvates - pharmacology
Skeletal muscle
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Lactate dehydrogenases at physiological concentrations are inhibited by high concentrations of pyruvate when the enzyme and the pyruvate are incubated in the presence of oxidized nicotinamide-adenine dinucleotide before assay. The inhibition is much more pronounced with the H-type than with the M-type lactate dehydrogenase. These results suggest that substrate inhibition may be operative in vivo.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.168.3936.1236