Cat No.
DIA-207
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 (Microorganism)
Alias
LDH; LD
Species
Microorganism
Enzyme Commission Number
EC 1.1.1.27
Bio-activity
GradeⅡ 400U/mg-solid or more
Appearance
White amorphous powder, lyophilized
Molecular Mass
approx. 140 kDa (by gel filtration)
pH Stability
pH 5.0-9.0 (25°C, 48hr)
Michaelis Constant
1.6×10??M (pyruvate, pH 7.0)
Isoelectric point
4
Optimum pH
6.0-7.0
Optimum temperature
35-40°C
Thermal stability
below 45°C (pH 7.0, 15min)
Stability
Store at-20°C
Inhibitors
Ag?, Hg??, SH-reagents
Applications
This enzyme is useful for enzymatic determination of numerous metabolites, e.g.ATP, ADP, glucose, creatinine, pyruvate, lactate and glycerol, and of enzyme activities, e.g.GPT, PK and CPK when coupled with the related enzymes.
Synonyms
Lactate dehydrogenase; EC 1.1.1.27; LDH; LD
