Lactate dehydrogenase 5 (LDH-5) is one of the major isoenzymes catalyzing the biochemical process of pyruvate to lactate. The purpose of this study was to investigate the expression of serum LDH-5 and test whether this enzyme is regulated by tumor hypoxia and represents a prognostic marker in patients with Non-Hodgkin's lymphoma (NHL). In this study, LDH-5 levels were detected using agarose gel...

Differential expression of isozymes enables fish to tolerate temperature fluctuations in their environment. The present study explores the modulation lactate dehydrogenase (LDH) and cytoplasmic malate (sMDH) isozyme heart, muscle, brain, liver, gill, kidney juvenile Horabagrus brachysoma after 30 days acclimation at 26, 31, 33, 36°C. LDH sMDH zymography were performed using native polyacrylamid...

The isozyme of lactate dehydrogenase (LDH) that is specific to testes, designated LDH-C4, is the predominant LDH isozyme in mammalian spermatozoa. Four high-affinity monoclonal antibodies have been developed to murine LDH-C4. These antibodies were tested for crossreactivity with LDH-C4 from rat, hamster, rabbit, and human by competitive binding radioimmunoassays. Monoclonal antibodies RG-1 and ...

Layered double hydroxide (LDH)@SiO2 nanoparticles were developed as a delivery carrier for the plasmid DNA expressing the Newcastle disease virus F gene. The LDH was hydrotalcite-like materials. The plasmid DNA encapsulated in the LDH@SiO2 nanoparticles (pFDNA-LDH@SiO2-NPs) was prepared by the coprecipitation method, and the properties of pFDNA-LDH@SiO2-NPs were characterized by transmission el...

Lactate dehydrogenase (LDH: 3.1.1.27) is a tetrameric enzyme participates in carbohydrate metabolism by catalyzing the oxidation of lactate and reduction of pyruvate. The random tetramerization of LDH-A and -B subunits leads to the formation of five tetramers: LDHB4, LDH-A1B3, LDH-A2B2, LDH-A3B1 and LDH-A4. Due to the biochemical and evolutionary significance of LDH isoenzyme characters or LDH ...

Lactate dehydrogenase (LDH; E.C. 1.1.1.27) is a crucial enzyme involved in energy metabolism in muscle, facilitating the production of ATP via glycolysis during oxygen deprivation by recycling NAD(+). The present study investigated purified LDH from the muscle of 20 h anoxic and normoxic T. s. elegans, and LDH from anoxic muscle showed a significantly lower (47%) K m for L-lactate and a higher ...

This note compares the substrate specificity of D-lactate dehydrogenase (D-LDH, EC 1.1.1.28) to that of L-lactate dehydrogenase (L-LDH, EC 1.1.1.27), illustrates three procedures that use D-LDH in synthesis and two methods for recycling NADH, and provides experimental details illustrating the use of D-LDH in organic synthesis.