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Topic:Malate Dehydrogenase

Malate dehydrogenase is an enzyme involved in the citric acid cycle, playing a role in the interconversion of malate and oxaloacetate. In horses, this enzyme is present in various tissues and is essential for cellular energy production and metabolic processes. It participates in both aerobic and anaerobic respiration, contributing to the regulation of energy supply during different physiological states. Malate dehydrogenase activity can be indicative of metabolic function and is studied in relation to equine muscle physiology, exercise performance, and metabolic disorders. This page compiles peer-reviewed research studies and scholarly articles that explore the structure, function, and clinical relevance of malate dehydrogenase in equine biology.
Aging effect on plasma metabolites and hormones concentrations in riding horses.
Open veterinary journal    November 2, 2015   Volume 5, Issue 2 154-157 
Kawasumi K, Yamamoto M, Koide M, Okada Y, Mori N, Yamamoto I, Arai T.Age effects on plasma metabolites, hormone concentrations, and enzyme activities related to energy metabolism were investigated in 20 riding horses. Animals were divided into two groups: Young (3-8 years) and aged (11-18 years). They were clinically healthy, and not obese. Plasma adiponectin (ADN) concentrations in aged horses were significantly lower than those in young horses (mean±SE, 6.5±1.3 µg mL(-1) vs, 10.9±1.7 µg mL(-1), Mann-Whitney U test, respectively; P=0.0233). Plasma non-esterified fatty acid levels and Insulin and malondialdehyde concentrations in aged group tended to incre...
Isoelectric focusing of some enzymes from Echinococcus granulosus (horse and sheep strains) and E. multilocularis.
Transactions of the Royal Society of Tropical Medicine and Hygiene    January 1, 1979   Volume 73, Issue 3 259-265 doi: 10.1016/0035-9203(79)90079-8
McManus DP, Smyth JD.Extracts of the horse and sheep strains of Echinococcus granulosus and E. multilocularis were compared on the basis of their isoenzyme patterns for 10 enzymes by means of isoelectric focusing in polyacrylamide gels. The enzymes examined were: acid phosphatase, lactate dehydrogenase, malate dehydrogenase, malic enzyme, phosphoglucoseisomerase, isocitrate dehydrogenase, adenylate kinase, aldolase and alpha-glycerophosphate dehydrogenase. Interspecific and intraspecific differences are apparent in the isoenzyme profiles of all the enzymes except adenylate kinase; the pattern and activity of adeny...