Lactate Dehydrogenase

Abstract

Lactate dehydrogenise is an important enzyme which is involved in carbohydrate metabolism. At the end of glycol sis , a molecule of glucose is broken in to two molecules of private with two molecules of cofactors (NADH+H?).NAD+ (Nicotinamide Adenine Dinucleotide radical) are involved in different steps for the removal to NADH+H+. The two molecules of pyruvate enter into the mitochondrial aerobic breakdown via kerb’s cycle .The reduced enzymes also enter the mitochondrial membrane to get oxidised back to NAD by atmospheric oxygen via electron transport system .if the supply of oxygen is interrupted , or some inhibition in the enzyme system occur..... or the rate of the aerobic breakdown of carbohydrates in response to grater metabolic demand exceeds the oxidative phase, NDA+ available in cytoplasm tends to get exhausted, in order to cope with this ,the NADH molecules formed as a result of glycol tic demand exceeds the oxidised from of NAD+ molecules ,the reactions takes place in place of the enzyme lactate dehydrogenise. Reaction is as follows. Which occurs in both direction (reversible reaction). CH?.CO.COO?+NADH+H?⇔CH?.CHOH.COO?+NAD? Pyruvate Lactate This reaction is catalysed by lactate dehydrogenises as such , in various sorts of stress conditions including the chemical stress .more lactate dehydrogenises level in the body is expected than in the normal condition. This enzyme is also interesting in showing iso enzyme patterns under different condition .As revealed by gel electrophoresis. it has been shown to exist in five molecular forms of iso enzymes’ of locate dehydrogenises are cloud be indentified in human serum , fish and other animals (An as tasi and banister ,1980,Radhian 1989) Kaplan (1963) and market (1955) demonstrated that these forms of two different sub units. These sub units have been designated as A and B by marker (1955) and as M and H BY KAPLAN (1963) .The five verities would ,therefore , be jermed A?Bo A?B?,A?B?,A?B?,A?B? according to market and according to Kaplan as lactate dehydrogenise 1 to 5 as LDH-1, LDH-2 , LDH-3,LDH-4, and LDH-5,.The LDA-1, most cathodic where as LDH-5,is most anodic. In human serum the normal range of LDH is 70-240 I .U. per litter (king.1960). LDH is widely distributed, being found in all cells in man but it is especially plentiful in cardiac and skeletal musicales, liver, kidney, and red blood cells. An increasing serum lactate dehydrogenises is found in myocardial infarction. An increase activity has also been found in liver disease, particularly I infective hepatitis