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LACTATE DEHYDROGENASE ENZYME AND ITS IMPLICATIONS IN CHEMICAL STRESS SITUATIONS
Abstract
Enzymes are major components of organism defense against toxic chemicals in their environment. Despite the passage of more than 200 million years of life presence these enzymes now play an important role in detoxifying chemicals man-made addiction and it may be a useful biomarker. Lactate dehydrogenase (LDH or LD) is intracellular enzyme year found early in all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvic acid to lactic acid and back, as it converts NAD + to NADH and back. A dehydrogenase enzyme transfers a hydride from one molecule to another. LDH enzyme exists in four distinct classes: first is NAD (P) -dependent L-lactate dehydrogenase; other LDHs act on D-lactic and / or is dependent on cytochome C: Dlactate dehydrogenase (cytochome) and L-lactate (L-lactate dehydrogenase (cytochome). LDH is expressed extensively in body tissues, such as blood cells and heart muscle. Lactate dehydrogenase (LDH) is widely distributed throughout the body, as seen mainly in the kidney, myocardium, skeletal muscle, brain, liver and lungs. Because it is released during tissue damage, it is a marker of common injuries such as heart failure and disease.
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References7
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