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Enzymes for Research, Diagnostic and Industrial Use

Native Porcine heart Lactate dehydrogenase

Cat No.
DIA-206
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 (Porcine)
Alias
LDH; LD
Source
Porcine heart
Species
Porcine
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.
Appearance
Crystalline suspension in 1.6M ammonium sulfate solution
Enzyme Commission Number
EC 1.1.1.27
Activity
GradeⅡ 2,000U/ml or more
CAS No.
9001-60-9
Contaminants
Malate dehydrogenase < 5.0×10⁻²% Pyruvate kinase < 3.0×10⁻²% GPT < 3.0×10⁻²%
Molecular Weight
115 kDa±6,500
pH Stability
pH 6.0-8.0(23°C, 22hr)
Michaelis Constant
2.5×10⁻²M (Lactate), 1.0×10⁻⁴M (Pyruvate)
Optimum pH
6.0-7.4
Optimum temperature
above 60°C
Thermal stability
below 50°C(pH 7.4, 10min)
Stability
Stable at 5°C for at least one year
Stabilizers
NADH, 2-mercaptoethanol
Inhibitors
I ‾, Ag⁺, Hg⁺⁺, p-chloromercuribenzoate, LDH inhibitors (formed from NADH)
Synonyms
Lactate dehydrogenase; EC 1.1.1.27; LDH; LD
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