Disease relevance of ldh-1

• The evolutionary relationships among 36 LDH isozymes from mammals, birds, amphibian, fish, nematode, plants, bacteria, mycoplasma and plasmodium were analyzed [1].
• Aqueous aspiration revealed normal lactate dehydrogenase levels and large numbers of eosinophils, suggesting the diagnosis of nematode endophthalmitis [2].

High impact information on ldh-1

• The nucleotide and deduced amino-acid sequences of a cDNA encoding lactate dehydrogenase from Caenorhabditis elegans: the evolutionary relationships of lactate dehydrogenases from mammals, birds, amphibian, fish, nematode, plants, bacteria, mycoplasma, and plasmodium [1].
• This first invertebrate LDH sequence of 333 amino acids, including the initiation methionine, exhibits 63% identity with that of the most primitive vertebrate lamprey [1].
• The intracellular distribution and high levels of activity observed for the enzymes phosphoenolpyruvate carboxykinase, pyruvate kinase, lactate dehydrogenase, malate dehydrogenase, malic enzyme and fumarate reductase suggest two alternative pathways of carbohydrate energy metabolism [3].
• The cytotoxic effect is a result of the destruction of the cell membrane, as shown by measuring the release of lactate dehydrogenase (LDH) [4].
• CF was cytotoxic with an IC50 approximately 730 and approximately 640 microm when assessed by the lactate dehydrogenase (LDH) assay and propidium iodide (PI) staining, respectively, 3 days after treatment [5].

Biological context of ldh-1

• A comparison of this genomic sequence with the published sequence of nematode LDH cDNA reveals the presence of two introns of 57 and 47 nucleotides at codon no [6].

Analytical, diagnostic and therapeutic context of ldh-1

• Furthermore, the isoenzymatic pattern of Lactate Dehydrogenase (LDH) has been studied in two different geographical strains of D. filaria and P. rufescens and in D. viviparus by starch gel electrophoresis [7].

References