The Experts below are selected from a list of 72 Experts worldwide ranked by ideXlab platform
Viroj Wiwanitkit - One of the best experts on this subject based on the ideXlab platform.
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Plasmodium and Host Lactate Dehydrogenase Molecular Function and Biological Pathways: Implication for Antimalarial Drug Discovery
Chemical biology & drug design, 2007Co-Authors: Viroj WiwanitkitAbstract:Lactate Dehydrogenase is an enzyme that catalyses the interconversion of pyruvate and Lactate with concomitant interconversion of NADH and NAD(+). Lactate Dehydrogenase is present at high levels in humans and Plasmodium spp. However, the function of Lactate Dehydrogenase in malarial infection is not well characterized. In this investigation, a new gene ontology technology is used to predict molecular function and biological pathways of Lactate Dehydrogenase. In comparison with human Lactate Dehydrogenase, the P. falciparum Lactate Dehydrogenase has similar molecular functions such as L-Lactate Dehydrogenase activity. Furthermore, P. falciparum Lactate Dehydrogenase has L-malate Dehydrogenase activity. Although the amino acid sequences for human and P. falciparum Lactate Dehydrogenase are very different, the molecular functions are similar. This suggests that any non-selective therapeutic treatment aimed at blocking P. falciparum Lactate Dehydrogenase function may affect human Lactate Dehydrogenase. In contrast, a selective Lactate Dehydrogenase inhibitor targeting the l-malate Dehydrogenase function of P. falciparum and its corresponding tricarboxylic acid cycle provides an attractive therapeutic opportunity.
William Nel - One of the best experts on this subject based on the ideXlab platform.
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EFFECTS OF COLD ACCLIMATION ON THE ACTIVITY LEVELS OF CREATINE KINASE, Lactate Dehydrogenase AND Lactate Dehydrogenase ISOENZYMES IN VARIOUS TISSUES OF THE RAT
Cell biology international, 1998Co-Authors: Stephanus E. Terblanche, T.c. Masondo, William NelAbstract:Abstract The effects of cold acclimation on the activity levels of creatine kinase, Lactate Dehydrogenase and Lactate Dehydrogenase isoenzymes in various tissues/ organs of the rat ( Rattus norvegicus ) were investigated. Male Sprague-Dawley rats were divided into two groups. One group was housed at 4±1°C (experimental group) and the other at 24±1°C (control group) for six months. The rats were housed in single cages and had access to food and water ad libitum. The tissues/organs investigated were heart, liver, lung, kidney, gastrocnemius muscle and interscapular brown adipose tissue as well as serum. With the exception of lung, (which showed a decrease of 24%) total creatine kinase activity levels were significantly increased ( P 0.05) in all the tissues/organs investigated (17–51%) as well as serum (34%), in cold acclimated animals. Cold acclimation also resulted in significantly increased ( P 0.05) activity levels of Lactate Dehydrogenase in all the tissues/organs investigated (14–24%) as well as serum (35%). Cold exposure resulted in an increase of the activity levels of all the detectable isoenzymes of Lactate Dehydrogenase, although not always significant, in all the tissues/organs investigated as well as serum. The M 4 tetramer of Lactate Dehydrogenase was the only detectable isoenzyme in serum.
Stephanus E. Terblanche - One of the best experts on this subject based on the ideXlab platform.
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EFFECTS OF COLD ACCLIMATION ON THE ACTIVITY LEVELS OF CREATINE KINASE, Lactate Dehydrogenase AND Lactate Dehydrogenase ISOENZYMES IN VARIOUS TISSUES OF THE RAT
Cell biology international, 1998Co-Authors: Stephanus E. Terblanche, T.c. Masondo, William NelAbstract:Abstract The effects of cold acclimation on the activity levels of creatine kinase, Lactate Dehydrogenase and Lactate Dehydrogenase isoenzymes in various tissues/ organs of the rat ( Rattus norvegicus ) were investigated. Male Sprague-Dawley rats were divided into two groups. One group was housed at 4±1°C (experimental group) and the other at 24±1°C (control group) for six months. The rats were housed in single cages and had access to food and water ad libitum. The tissues/organs investigated were heart, liver, lung, kidney, gastrocnemius muscle and interscapular brown adipose tissue as well as serum. With the exception of lung, (which showed a decrease of 24%) total creatine kinase activity levels were significantly increased ( P 0.05) in all the tissues/organs investigated (17–51%) as well as serum (34%), in cold acclimated animals. Cold acclimation also resulted in significantly increased ( P 0.05) activity levels of Lactate Dehydrogenase in all the tissues/organs investigated (14–24%) as well as serum (35%). Cold exposure resulted in an increase of the activity levels of all the detectable isoenzymes of Lactate Dehydrogenase, although not always significant, in all the tissues/organs investigated as well as serum. The M 4 tetramer of Lactate Dehydrogenase was the only detectable isoenzyme in serum.
Debasish Chattopadhyay - One of the best experts on this subject based on the ideXlab platform.
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Biochemical and structural characterization of Cryptosporidium parvum Lactate Dehydrogenase.
International journal of biological macromolecules, 2014Co-Authors: William J. Cook, Olga Senkovich, Agustín Hernández, Haley E. Speed, Debasish ChattopadhyayAbstract:The protozoan parasite Cryptosporidium parvum causes waterborne diseases worldwide. There is no effective therapy for C. parvum infection. The parasite depends mainly on glycolysis for energy production. Lactate Dehydrogenase is a major regulator of glycolysis. This paper describes the biochemical characterization of C. parvum Lactate Dehydrogenase and high resolution crystal structures of the apo-enzyme and four ternary complexes. The ternary complexes capture the enzyme bound to NAD/NADH or its 3-acetylpyridine analog in the cofactor binding pocket, while the substrate binding site is occupied by one of the following ligands: Lactate, pyruvate or oxamate. The results reveal distinctive features of the parasitic enzyme. For example, C. parvum Lactate Dehydrogenase prefers the acetylpyridine analog of NADH as a cofactor. Moreover, it is slightly less sensitive to gossypol inhibition compared with mammalian Lactate Dehydrogenases and not inhibited by excess pyruvate. The active site loop and the antigenic loop in C. parvum Lactate Dehydrogenase are considerably different from those in the human counterpart. Structural features and enzymatic properties of C. parvum Lactate Dehydrogenase are similar to enzymes from related parasites. Structural comparison with malate Dehydrogenase supports a common ancestry for the two genes.
E Bogin - One of the best experts on this subject based on the ideXlab platform.
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Lactate Dehydrogenase isoenzyme distribution and patterns in chicken organs.
Research in veterinary science, 1999Co-Authors: D Heinova, I Rosival, Y Avidar, E BoginAbstract:Unlike most mammals, chicken Lactate Dehydrogenase isoenzymes cannot be separated using the 'Titan-Gel' electrophoresis. However, using isoelectric focusing at a pH range of 3.0 to 9.0, a good and clear separation of all five isoenzymes was achieved. Generally, three characteristic groups were seen: (a) those having a cathodic domination (breast muscle and serum) with mainly Lactate Dehydrogenase-5 (b) those having an anodic domination (heart, muscle, liver, pancreas, kidney, erythrocytes) of mainly Lactate Dehydrogenase - 1 and 2 and (c) those with a more uniform distribution (spleen, lung, and brain). The total Lactate Dehydrogenase activity was the highest in the breast muscle, followed by the heart muscle, liver and serum with the lowest activities in the lung and pancreas.
