Cat No.
DIA-268
Description
A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.
Abbr
LDH (Rabbit)
Alias
LDH; LD
Source
Rabbit Muscle
Species
Rabbit
Enzyme Commission Number
EC 1.1.1.27
Bio-activity
> 250 units per mg protein
Molecular Mass
140 kDa
Composition
Lovell and Winzor (1974) report that the tetramer dissociates completely into two dimers (molecular weight 70,000) in acetate-chloride buffer pH 5 (conditions without effect on beef heart LDH). Phosphate and pyridine nucleotides stabilize the quarternary structure of the tetramer. Phosphate has an activation effect. See also Cho and Swainsgood (1973).
Unit Definition
One Unit oxidizes one micromole of NADH per minute at 25°C, pH 7.3
Synonyms
Lactate dehydrogenase; EC 1.1.1.27; LDH; LD
