Native Microorganism D-lactate dehydrogenase
| Cat# | DIA-207 |
| Abbr | LDH (Microorganism) |
| Alias | LDH; LD |
| Source | Microorganism |
| 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. |
| 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 |
| Form | Freeze dried powder |
| Enzyme Commission Number | EC 1.1.1.27 |
| Activity | 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% |
| 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) |
| Storage | Store at -20°C |
| Synonyms | Lactate dehydrogenase; EC 1.1.1.27; LDH; LD |
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