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Native Microorganism D-lactate dehydrogenase

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
Source
Microorganism
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
White amorphous powder, lyophilized
Enzyme Commission Number
EC 1.1.1.27
Activity
GradeⅡ 400U/mg-solid or more
CAS No.
9001-60-9
Contaminants
NADH oxidase < 1.0×10⁻³% Malate dehydrogenase < 1.0×10⁻²% GOT < 5.0×10⁻³% GPT < 5.0×10⁻³% Myokinase < 1.0×10⁻²% Pyruvate kinase< 1.0×10⁻³%
Molecular Weight
approx. 140 kDa (by gel filtration)
Isoelectric point
4
pH Stability
pH 5.0-9.0 (25°C, 48hr)
Michaelis Constant
1.6×10⁻⁴M (pyruvate, pH 7.0)
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
Synonyms
Lactate dehydrogenase; EC 1.1.1.27; LDH; LD
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Realted Products
Catalog
ProductName
EC No.
CAS No.
Source
Price
CatalogNATE-1680
EC No.EC 1.1.1.27
CAS No.9001-60-9
SourceHuman Heart
CatalogNATE-1681
EC No.EC 1.1.1.27
CAS No.9001-60-9
SourceHuman Muscle
CatalogNATE-1793
EC No.EC 1.1.1.27
CAS No.9001-60-9
SourceE. coli
CatalogDIA-206
EC No.EC 1.1.1.27
CAS No.9001-60-9
SourcePorcine heart
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Realted Service
Realted Protocols
L-LACTIC DEHYDROGENASE -Enzymatic Assay Protocol
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