L-Lactic dehydrogenase

Base Information

• Chemical Name: L-Lactic dehydrogenase
• CAS No.: 9001-60-9
• Molecular Formula: NULL
• Molecular Weight: 0
• Hs Code.: 35079090
• Mol file: 9001-60-9.mol

Synonyms:(S)-Lactatedehydrogenase;E.C. 1.1.1.27;L-Lactate dehydrogenase;L-Lactic aciddehydrogenase;L-Lactic dehydrogenase;Lactate dehydrogenase;Lactatedehydrogenase NAD-dependent;Lactic acid dehydrogenase;Lactic dehydrogenase;NAD-lactate dehydrogenase;NADH-dependent lactate dehydrogenase;Proteins,anoxic stress response, p34;

Chemical Property of L-Lactic dehydrogenase

Chemical Property:

• Appearance/Colour: white
• PSA: 0.00000
• LogP: 0.00000
• Storage Temp.: 2-8°C

Purity/Quality:

99%, ^*data from raw suppliers

Lactate Dehydrogenase ^*data from reagent suppliers

Safty Information:

• Statements: 21/22-36/37/38
• Safety Statements: 22-24/25-36/37-26

MSDS Files:

SDS file from LookChem

Useful:

• Uses: L-Lactic dehydrogenase is used in the determination of pyruvate (used in conjunction with reduced coenzyme) and in the diagnosis of myocardial infarction and leukemia. L-Lactic Dehydrogenase from bovine heart has been used as a standard in cytotoxicity assay. It has also been used in glutamic pyruvic transaminase (GPT) assay. L-Lactic Dehydrogenase from bovine heart has been used in ATPase assay of R2 complex Rvb1p-Rvb2p, RecA protein and sarcoplasmic reticulum Ca2+-ATPase (SERCA).

Refernces

SYNTHESIS AND PROPERTIES OF A NEW NAD ANALOG: AMINOETHYLNICOTINAMIDE ADENINE DINUCLEOTIDE

10.1007/BF00772217

The study focuses on the synthesis and properties of a new NAD analog, aminoethylnicotinamide adenine dinucleotide (AE-NAD). The researchers synthesized AE-NAD through an exchange reaction of transglycosylation from NAD and N'-aminoethylnicotinamide in the presence of pig spleen β-NAD-transglycohydrolase. The study aims to examine the properties of AE-NAD and its ability to interact with yeast glyceraldehyde-3-phosphate dehydrogenase (GAPD), yeast alcohol dehydrogenase (ADH), and pig muscle M4 lactate dehydrogenase (LDH) isoenzyme. The results show that AE-NAD has an electrophilicity of the pyridine ring similar to NAD and favors an unfolded conformation in solution, which should facilitate its interaction with dehydrogenase active centers. However, AE-NAD does not form the reduced form in the presence of GAPD, ADH, or LDH, and it has a weak inhibitory effect on LDH-catalyzed reactions, possibly due to the disruption of dinucleotide binding at the active center of the enzyme.