Product name:Lactate dehydrogenase
CAS:9001-60-9
Specification:100mg
Description:
Lactate dehydrogenase (LDH or LD) is an enzyme (EC 1.1.1.27) present in a wide variety of organisms, including plants and animals.
Lactate dehydrogenases exist in four distinct enzyme classes. Two of them are cytochrome c-dependent enzymes with each acting on either D-lactate (EC 1.1.2.4) or L-lactate (EC 1.1.2.3). The other two are NAD(P)-dependent enzymes with each acting on either D-lactate (EC 1.1.1.28) or L-lactate (EC 1.1.1.27). This article is about the NAD(P)-dependent L-lactate dehydrogenase.
Lactate dehydrogenase is white freeze dried powder or 3.2mol/L ammonium sulfate crystalline suspension, soluble in water, pI 4.6, optimal pH 6.0. Stability: crystallization enzyme solution can be stored for 6-8 weeks without changing activity, sulfate suspension can be stable for more than a year, very dilute solution is unstable; The optimal temperature is 39℃, and the rapid deactivation occurs when the temperature is higher than 60℃. Inhibitors have a surfeit of pyruvate, excessive NAD, oxalic acid, oxalic acid amide, hydroxy malonic acid, malonic acid, urea, Cu2 +, Hg2 +, Ag +, mercury chloride, benzoic acid, 4 - pyrophosphate or and in alkaline phosphate buffer from coenzyme I (NAD) formed a non-competitive inhibitors have inhibitory effect on the oxidation reaction, excess lactic acid and formed from the reduced coenzyme I (NADH) non-competitive inhibitors have inhibitory effect on reduction reaction; Activators include 2-amino2-methyl-1-propanol, fluoride, diethanolamine, and heparin (oxidation). Enzyme reaction: pyruvic acid salt + reduced coenzyme I + H + + coenzyme I ═ lactic acid salt.
Lactate dehydrogenase is used for biochemical research, determination of pyruvate, diagnosis of leukemia and myocardial infarction.
Lactate dehydrogenase USES pig heart as raw material, through calcium phosphate gel treatment, ammonium sulfate grade precipitation, after dialysis, ammonium sulfate crystallization products.