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Статті в журналах з теми "Lactate dehydrogenase"

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Автор: Grafiati

Опубліковано: 4 червня 2021

Оновлено: 10 березня 2023

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1

Rehse, Peter H., and William S. Davidson. "Evolutionary Relationship of a Fish C Type Lactate Dehydrogenase to Other Vertebrate Lactate Dehydrogenase Isozymes." Canadian Journal of Fisheries and Aquatic Sciences 43, no. 5 (May 1, 1986): 1045–51. http://dx.doi.org/10.1139/f86-130.

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It is assumed that the genes for the three types of vertebrate lactate dehydrogenase isozymes (A, B, and C) arose from an ancestral lactate dehydrogenase gene by a mechanism involving gene duplications. The currently accepted model was originally proposed by Holmes in 1972 (FEBS Lett. 28: 51–55). The main points in this proposal are as follows: (1) the ancestral lactate dehydrogenase was an A type; (2) the gene for this A type lactate dehydrogenase duplicated to produce the A and B forms; and (3) the C isozymes of fish and warm-blooded vertebrates are derived from B types by successive, independent gene duplication events. More structural data have become available since this model was first put forward, and Li et al. (1983. J. Biol. Chem. 258: 7029–7032) have shown that rodent C type lactate dehydrogenases appear to be ancestral to the A and B forms. We have extended Li's reevaluation of the evolutionary relationships among vertebrate lactate dehydrogenase isozymes. Our analysis indicates that there is no significant difference in the rates of evolution along the A, B, or C lineages. This confirms that a C type rather than an A type lactate dehydrogenase was the ancestral form. A duplication of the gene for this C type gave rise to the gene which, by a further gene duplication, yielded the A and B type lactate dehydrogenase genes. In addition, amino acid compositional data reveal that the C type lactate dehydrogenase from Atlantic cod (Gadus morhua) and the C type lactate dehydrogenase isozymes of rodents are homologous proteins that are the result of divergent evolution via speciation events rather than by independent gene duplications. This novel interpretation of lactate dehydrogenase isozyme evolution is discussed with respect to the tissue specificities of C type lactate dehydrogenases in vertebrates.

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2

Anand, Usha. "Lactate Dehydrogenase." Clinical Chemistry 59, no. 3 (March 1, 2013): 585. http://dx.doi.org/10.1373/clinchem.2011.178541.

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3

Allison, N., M. J. O'Donnell, M. E. Hoey, and C. A. Fewson. "Membrane-bound lactate dehydrogenases and mandelate dehydrogenases of Acinetobacter calcoaceticus. Location and regulation of expression." Biochemical Journal 227, no. 3 (May 1, 1985): 753–57. http://dx.doi.org/10.1042/bj2270753.

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Acinetobacter calcoaceticus possesses an L(+)-lactate dehydrogenase and a D(-)-lactate dehydrogenase. Results of experiments in which enzyme activities were measured after growth of bacteria in different media indicated that the two enzymes were co-ordinately induced by either enantiomer of lactate but not by pyruvate, and repressed by succinate or L-glutamate. The two lactate dehydrogenases have very similar properties to L(+)-mandelate dehydrogenase and D(-)-mandelate dehydrogenase. All four enzymes are NAD(P)-independent and were found to be integral components of the cytoplasmic membrane. The enzymes could be solubilized in active form by detergents; Triton X-100 or Lubrol PX were particularly effective D(-)-Lactate dehydrogenase and D(-)-mandelate dehydrogenase could be selectively solubilized by the ionic detergents cholate, deoxycholate and sodium dodecyl sulphate.

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4

Oren, Aharon, and Peter Gurevich. "Diversity of lactate metabolism in halophilic archaea." Canadian Journal of Microbiology 41, no. 3 (March 1, 1995): 302–7. http://dx.doi.org/10.1139/m95-042.

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D-Lactate is readily used as a substrate for the growth of species of halophilic archaea belonging to the genera Haloferax and Haloarcula. L-Lactate was used by Haloferax species (Haloferax volcanii, Haloferax mediterranei) only when a substantial concentration of the D-isomer was also present in the medium. On the enzymatic level, considerable diversity was found in the lactate metabolism of the different representatives of the Halobacteriaceae. At least three types of lactate dehydrogenases were detected in halophilic archaea. A high level of activity of an NAD-linked enzyme was present constitutively in Haloarcula species, and a low level of activity was also detected in Haloferax mediterranei. NAD-independent lactate dehydrogenases, oxidizing L-lactate and D-lactate with 2,6-dichlorophenol-indophenol as electron acceptor, were detected in all nine species tested, but L-lactate dehydrogenase activity in Halobacterium species was very low, and Haloarcula species, which possess a high level of activity of NAD-linked lactate dehydrogenase, showed very low activities of both NAD-independent D- and L-lactate dehydrogenase. An inducible lactate racemase, displaying an unusually high pH optimum, was found in Haloferax volcanii. Lactate racemase activity was found constitutively in Haloarcula species, but no activity was detected in Halobacterium species and in Haloferax mediterranei.Key words: lactate dehydrogenase, lactate racemase, Halobacterium, Haloferax, Haloarcula.

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5

Vind, C., A. Hunding, and N. Grunnet. "Pathways of reducing equivalents in hepatocytes from rats. Estimation of cytosolic fluxes by means of 3H-labelled substrates for either A- or B-specific dehydrogenases." Biochemical Journal 243, no. 3 (May 1, 1987): 625–30. http://dx.doi.org/10.1042/bj2430625.

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The metabolism of [2-3H]lactate and [2-3H]glycerol was studied in isolated hepatocytes from fed rats. In order to estimate the rate of equilibrium between the 4A and 4B hydrogen atoms of NADH, we compared the flow of 3H from [2-3H]lactate and [2-3H]glycerol, the oxidations of which are catalysed by A- and B-type dehydrogenases, respectively. Hepatocytes were incubated with lactate, glycerol and ethanol and tracer amounts of [2-3H]lactate or [2-3H]glycerol and the labelling rates of lactate, ethanol, glucose and glycerol phosphate were determined. The data were used to calculate the oxidation rate of NADH catalysed by lactate dehydrogenase, alcohol dehydrogenase, triosephosphate dehydrogenase and glycerol phosphate dehydrogenase. The rates were calculated by obtaining the best fit of a model to the experimental data by using a least-squares procedure. The results support our model and suggest that the fluxes through various dehydrogenases are sufficient to equilibrate the 4A and 4B hydrogen atoms of cytosolic NADH. The validity of the metabolic models used was evaluated by comparison of rates of NADH oxidation catalysed by cytosolic dehydrogenases as calculated by two different models.

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6

Maekawa, Masato. "Lactate dehydrogenase isoenzymes." Journal of Chromatography B: Biomedical Sciences and Applications 429 (July 1988): 373–98. http://dx.doi.org/10.1016/s0378-4347(00)83879-7.

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7

Simon, Ethan S., Raymond Plante, and George M. Whitesides. "D-lactate dehydrogenase." Applied Biochemistry and Biotechnology 22, no. 2 (November 1989): 169–79. http://dx.doi.org/10.1007/bf02921743.

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8

Wolf, Paul L. "Lactate Dehydrogenase—6." Archives of Internal Medicine 145, no. 8 (August 1, 1985): 1396. http://dx.doi.org/10.1001/archinte.1985.00360080066008.

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9

Kovář, Jan, Alena Škodová, and Jaroslav Turánek. "The use of Spheron as a matrix for affinity chromatography of NAD-dependent dehydrogenases." Collection of Czechoslovak Chemical Communications 51, no. 7 (1986): 1542–49. http://dx.doi.org/10.1135/cccc19861542.

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The paper compares several methods of coupling common ligands of dehydrogenases, viz. N6-[(6-aminohexyl)carbamoylmethyl]-AMP and N6-[(6-aminohexyl)carbamoylmethyl]-NAD, to a hydrophilic macroporous glycolmethacrylate gel, Spheron. The affinants coupled best to a CNBr-activated gel and to a gel with hydrazine groups (after activation with nitrous acid). The affinity properties of gels based on Spheron and on Sepharose 4B were similar ( the stability and separation efficiency were almost identical, the binding capacity and the recovery of dehydrogenase activity were somewhat better with the Sepharose). The materials based on Spheron were used in several separation experiments, viz. separation of lactate dehydrogenase form albumin, separation of lactate dehydrogenase from alcohol dehydrogenase under different conditions and separation of isoenzymes of lactate dehydrogenase. Spheron 300 with a coupled affinant was also employed in an attempt to purify a crude alcohol dehydrogenase.

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10

Sass, C., M. Briand, S. Benslimane, M. Renaud, and Y. Briand. "Characterization of Rabbit Lactate Dehydrogenase-M and Lactate Dehydrogenase-H cDNAs." Journal of Biological Chemistry 264, no. 7 (March 1989): 4076–81. http://dx.doi.org/10.1016/s0021-9258(19)84964-5.

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11

Goffin, Philippe, Frédérique Lorquet, Michiel Kleerebezem, and Pascal Hols. "Major Role of NAD-Dependent Lactate Dehydrogenases in Aerobic Lactate Utilization in Lactobacillus plantarum during Early Stationary Phase." Journal of Bacteriology 186, no. 19 (October 1, 2004): 6661–66. http://dx.doi.org/10.1128/jb.186.19.6661-6666.2004.

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ABSTRACT NAD-independent lactate dehydrogenases are commonly thought to be responsible for lactate utilization during the stationary phase of aerobic growth in Lactobacillus plantarum. To substantiate this view, we constructed single and double knockout mutants for the corresponding genes, loxD and loxL. Lactate-to-acetate conversion was not impaired in these strains, while it was completely blocked in mutants deficient in NAD-dependent lactate dehydrogenase activities, encoded by the ldhD and ldhL genes. We conclude that NAD-dependent but not NAD-independent lactate dehydrogenases are involved in this process.

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12

Kelley, P. D., D. S. Brink, J. H. Joist, and D. Ritter. "Lactate dehydrogenase isoenzyme utilization." Clinical Chemistry 42, no. 10 (October 1, 1996): 1723–24. http://dx.doi.org/10.1093/clinchem/42.10.1723.

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13

Ichijima, Hideji, Masaki Imayasu, Jun-ichi Ohashi, and H. Dwight Cavanagh. "Tear Lactate Dehydrogenase Levels." Cornea 11, no. 2 (March 1992): 114–20. http://dx.doi.org/10.1097/00003226-199203000-00004.

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14

Ghosh, Kanjaksha. "Lactate Dehydrogenase in CML." American Journal of Clinical Pathology 99, no. 1 (January 1, 1993): 113. http://dx.doi.org/10.1093/ajcp/99.1.113.

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15

Rowson, K. E. K., and B. W. J. Mahy. "Lactate Dehydrogenase-elevating Virus." Journal of General Virology 66, no. 11 (November 1, 1985): 2297–312. http://dx.doi.org/10.1099/0022-1317-66-11-2297.

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16

Deck, Lorraine M., Robert E. Royer, Brian B. Chamblee, Valerie M. Hernandez, Richard R. Malone, Jose E. Torres, Lucy A. Hunsaker, Robert C. Piper, Michael T. Makler, and David L. Vander Jagt. "Selective Inhibitors of Human Lactate Dehydrogenases and Lactate Dehydrogenase from the Malarial ParasitePlasmodiumfalciparum." Journal of Medicinal Chemistry 41, no. 20 (September 1998): 3879–87. http://dx.doi.org/10.1021/jm980334n.

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17

Hua, Yibo, Chao Liang, Jundong Zhu, Chenkui Miao, Yajie Yu, Aimin Xu, Jianzhong Zhang, et al. "Expression of lactate dehydrogenase C correlates with poor prognosis in renal cell carcinoma." Tumor Biology 39, no. 3 (March 2017): 101042831769596. http://dx.doi.org/10.1177/1010428317695968.

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Lactate dehydrogenase C is an isoenzyme of lactate dehydrogenase and a member of the cancer–testis antigens family. In this study, we aimed to investigate the expression and functional role of lactate dehydrogenase C and its basic mechanisms in renal cell carcinoma. First, a total of 133 cases of renal cell carcinoma samples were analysed in a tissue microarray, and Kaplan–Meier survival curve analyses were performed to investigate the correlation between lactate dehydrogenase C expression and renal cell carcinoma progression. Lactate dehydrogenase C protein levels and messenger RNA levels were significantly upregulated in renal cell carcinoma tissues, and the patients with positive lactate dehydrogenase C expression had a shorter progression-free survival, indicating the oncogenic role of lactate dehydrogenase C in renal cell carcinoma. In addition, further cytological experiments demonstrated that lactate dehydrogenase C could prompt renal cell carcinoma cells to produce lactate, and increase metastatic and invasive potential of renal cell carcinoma cells. Furthermore, lactate dehydrogenase C could induce the epithelial–mesenchymal transition process and matrix metalloproteinase-9 expression. In summary, these findings showed lactate dehydrogenase C was associated with poor prognosis in renal cell carcinoma and played a pivotal role in the migration and invasion of renal cell carcinoma cells. Lactate dehydrogenase C may act as a novel biomarker for renal cell carcinoma progression and a potential therapeutic target for the treatment of renal cell carcinoma.

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18

Allison, N., M. J. O'Donnell, and C. A. Fewson. "Membrane-bound lactate dehydrogenases and mandelate dehydrogenases of Acinetobacter calcoaceticus. Purification and properties." Biochemical Journal 231, no. 2 (October 15, 1985): 407–16. http://dx.doi.org/10.1042/bj2310407.

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Procedures were developed for the optimal solubilization of D-lactate dehydrogenase, D-mandelate dehydrogenase, L-lactate dehydrogenase and L-mandelate dehydrogenase from wall + membrane fractions of Acinetobacter calcoaceticus. D-Lactate dehydrogenase and D-mandelate dehydrogenase were co-eluted on gel filtration, as were L-lactate dehydrogenase and L-mandelate dehydrogenase. All four enzymes could be separated by ion-exchange chromatography. D-Lactate dehydrogenase and D-mandelate dehydrogenase were purified by cholate extraction, (NH4)2SO4 fractionation, gel filtration, ion-exchange chromatography and chromatofocusing. The properties of D-lactate dehydrogenase and D-mandelate dehydrogenase were similar in several respects: they had relative molecular masses of 62 800 and 59 700 respectively, pI values of 5.8 and 5.5, considerable sensitivity to p-chloromercuribenzoate, little or no inhibition by chelating agents, and similar responses to pH. Both enzymes appeared to contain non-covalently bound FAD as cofactor.

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19

Chen, P.-P., S.-M. Tsai, H.-M. Wang, L.-F. Wang, C.-Y. Chien, N.-C. Chang, and K.-Y. Ho. "Lactate dehydrogenase isoenzyme patterns in auricular pseudocyst fluid." Journal of Laryngology & Otology 127, no. 5 (April 10, 2013): 479–82. http://dx.doi.org/10.1017/s0022215113000534.

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AbstractObjective:We investigated lactate dehydrogenase isoenzyme patterns in the cyst fluid of auricular pseudocysts and autogenous blood, to assist the diagnosis of auricular pseudocyst.Methods:Twenty patients with auricular pseudocysts participated in this study conducted in Kaohsiung Medical University Hospital between February 2007 and June 2010. Patterns of lactate dehydrogenase in cyst fluid and autogenous blood were analysed.Results:Levels of lactate dehydrogenase 1 and 2 were lower in auricular pseudocysts than in autogenous blood, whereas levels of lactate dehydrogenase 4 and 5 were higher; this difference was statistically significant (p < 0.001).Conclusion:Lactate dehydrogenase isoenzyme patterns in auricular pseudocyst fluid indicated higher percentage distributions of lactate dehydrogenase 4 and 5 and lower percentage distributions of lactate dehydrogenase 1 and 2. An effective laboratory method of evaluating the different lactate dehydrogenase isoenzyme components was developed; this method may improve the accuracy of auricular pseudocyst diagnosis.

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20

Sugawara, E., S. Yamamoto, and N. Hasegawa. "A case of immunoglobulin A-linked lactate dehydrogenase with high lactate dehydrogenase activity." Clinical Chemistry 31, no. 11 (November 1, 1985): 1920. http://dx.doi.org/10.1093/clinchem/31.11.1920.

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21

Kraaijenhagen, R. J., and E. T. Backer. "Reversible loss of lactate dehydrogenase isoenzymes and lactate dehydrogenase activity in patient's serum." Clinical Chemistry 34, no. 4 (April 1, 1988): 781–83. http://dx.doi.org/10.1093/clinchem/34.4.781.

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Abstract An abnormal lactate dehydrogenase (LD; EC 1.1.1.27) electrophoretogram (only one band, at the application site) and a low LD activity (7 U/L) was seen for a patient's serum during storage at 22 and 4 degrees C. Both reverted to normal when the serum was incubated at 37 degrees C.

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22

Zhu, Lingfeng, Xiaoling Xu, Limin Wang, Hui Dong, Bo Yu, and Yanhe Ma. "NADP+-Preferring d-Lactate Dehydrogenase from Sporolactobacillus inulinus." Applied and Environmental Microbiology 81, no. 18 (July 6, 2015): 6294–301. http://dx.doi.org/10.1128/aem.01871-15.

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ABSTRACTHydroxy acid dehydrogenases, includingl- andd-lactate dehydrogenases (L-LDH and D-LDH), are responsible for the stereospecific conversion of 2-keto acids to 2-hydroxyacids and extensively used in a wide range of biotechnological applications. A common feature of LDHs is their high specificity for NAD+as a cofactor. An LDH that could effectively use NADPH as a coenzyme could be an alternative enzymatic system for regeneration of the oxidized, phosphorylated cofactor. In this study, ad-lactate dehydrogenase from aSporolactobacillus inulinusstrain was found to use both NADH and NADPH with high efficiencies and with a preference for NADPH as its coenzyme, which is different from the coenzyme utilization of all previously reported LDHs. The biochemical properties of the D-LDH enzyme were determined by X-ray crystal structural characterization andin vivoandin vitroenzymatic activity analyses. The residue Asn174was demonstrated to be critical for NADPH utilization. Characterization of the biochemical properties of this enzyme will contribute to understanding of the catalytic mechanism and provide referential information for shifting the coenzyme utilization specificity of 2-hydroxyacid dehydrogenases.

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23

Milewski, W. M., S. Boyle-Vavra, B. Moreira, C. C. Ebert, and R. S. Daum. "Overproduction of a 37-kilodalton cytoplasmic protein homologous to NAD+-linked D-lactate dehydrogenase associated with vancomycin resistance in Staphylococcus aureus." Antimicrobial Agents and Chemotherapy 40, no. 1 (January 1996): 166–72. http://dx.doi.org/10.1128/aac.40.1.166.

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We previously reported the isolation of a laboratory-derived Staphylococcus aureus mutant, 523k, that has constitutive low-level resistance to vancomycin (MIC = 5 micrograms/ml) and teicoplanin (MIC = 5 micrograms/ml) and elaborates a ca. 39-kDa cytoplasmic protein that was not detected in the parent strain 523 (MIC = 1 micrograms/ml). We have now detected the protein in strain 523 by immunoblotting with antiserum raised against the protein. Consistent with our initial observations, densitometric analysis of the immunoblots revealed an increased production of the protein in 523k compared with that of the susceptible parent 523. The 5' region of the gene encoding the protein of interest was identified by nucleotide sequencing a PCR product amplified from the genome of 523k with degenerate primers designed to encode the amino acid sequence of proteolytic peptides obtained from the protein. The remainder of the gene was identified by library screening, PCR, and nucleotide sequencing. The gene encodes a 36.7-kDa protein with homology to a family of bacterial NAD+-dependent, D-specific 2-hydroxyacid dehydrogenases which includes both D-lactate dehydrogenase and the enterococcal vancomycin resistance protein VanH and is therefore designated ddh. Increased production of the product of ddh, Ddh, was associated with increased D-lactate dehydrogenase activity in 523k, a finding which suggested that Ddh is likely to be the D-lactate dehydrogenase previously identified in S. aureus. The increased D-lactate dehydrogenase activity in strain 523k and the structural similarities among Ddh, D-lactate dehydrogenase, and VanH suggest that overproduction of Ddh might play a role in vancomycin resistance in this strain.

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24

Triyono, Teguh, Umi Solekhah Intansari, and Caesar Haryo Bimoseno. "LACTATE DEHYDROGENASE (LDH) SELAMA PENYIMPANAN." INDONESIAN JOURNAL OF CLINICAL PATHOLOGY AND MEDICAL LABORATORY 19, no. 3 (October 14, 2016): 174. http://dx.doi.org/10.24293/ijcpml.v19i3.416.

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During storage, erythrocytes suffered from biomechanical alterations called the “storage lesion”, which may caused hemolysis. The hemolysis released LDH into the plasma. The LDH that was released during hemolysis made it an adequate instrument to assess the quality of in vitro blood products. The aims of this study were to analyse the alteration of LDH level at day 1, 3, 7, 14, and 28 in the WB and PRC, to analyse the correlation between LDH level with storage duration, and also to analyse enhancement differences of LDH level between WB and PRC.This research was an observational study with a cross-sectional design. As the samples there were 11 bags of WB and 10 bags of PRC. Blood products were kept in bloodbank with the temperature range of 2–6° C. The LDH level was measured with the Beckman Chemistry Analyzer. There were statistically significant alterations of LDH level started from day 7 of storage in both blood products (p<0.05). The significant strong correlation between LDH level with the storage duration were found r=0.772; r=0.835 (p<0.05) in WB and PRC respectively. The enhancement differences were found to be higher and significant in the PRC than in the WB started from day 7 of storage (p<0.05). As conclusion, LDH in WB and PRC were signifantly increased during storage, and correlate with storage duration.

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25

Mannen, Hideyuki. "Molecular Evolution of Lactate Dehydrogenase." Journal of animal genetics 25, no. 1 (1997): 21–26. http://dx.doi.org/10.5924/abgri1993.25.21.

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26

Gano, Lindsey B., and Manisha Patel. "Fermenting Seizures with Lactate Dehydrogenase." Epilepsy Currents 15, no. 5 (September 2015): 274–76. http://dx.doi.org/10.5698/1535-7511-15.5.274.

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27

Podlasek, Stanley J., and Richard A. McPherson. "New Lactate Dehydrogenase–IgM Complexes." Laboratory Medicine 20, no. 9 (September 1, 1989): 617–19. http://dx.doi.org/10.1093/labmed/20.9.617.

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28

Devgun, M. S. "Lactate dehydrogenase in lung cancer." Clinical Chemistry 34, no. 9 (September 1, 1988): 1947–48. http://dx.doi.org/10.1093/clinchem/34.9.1947a.

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29

Moezelaar, Roy, M. Joost Teixeira Mattos, and Lucas J. Stal. "Lactate dehydrogenase in the cyanobacteriumMicrocystisPCC7806." FEMS Microbiology Letters 127, no. 1-2 (March 1995): 47–50. http://dx.doi.org/10.1111/j.1574-6968.1995.tb07448.x.

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30

Jialal, Ishwarlal, and Lori J. Sokoll. "Clinical Utility of Lactate Dehydrogenase." American Journal of Clinical Pathology 143, no. 2 (February 1, 2015): 158–59. http://dx.doi.org/10.1309/ajctp0fc8qfydfa.

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31

Krechl, Jiří, and Svatava Smrčková. "Biomimetic models of lactate dehydrogenase." Tetrahedron Letters 30, no. 39 (January 1989): 5315–18. http://dx.doi.org/10.1016/s0040-4039(01)93774-8.

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32

King, Lan, and Gregorio Weber. "Conformational Drift of Lactate Dehydrogenase." Biophysical Journal 49, no. 1 (January 1986): 72–73. http://dx.doi.org/10.1016/s0006-3495(86)83597-4.

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33

Wolf, Paul L. "Interpretation of Lactate Dehydrogenase Isoenzymes." Clinics in Laboratory Medicine 6, no. 3 (September 1986): 541–45. http://dx.doi.org/10.1016/s0272-2712(18)30799-6.

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34

Livesey, A., F. Garty, A. R. Shipman, and K. E. Shipman. "Lactate dehydrogenase in dermatology practice." Clinical and Experimental Dermatology 45, no. 5 (November 21, 2019): 539–43. http://dx.doi.org/10.1111/ced.14134.

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35

Brandt, Richard B., Jerome E. Laux, Stephen E. Spainhour, and Edward S. Kline. "Lactate dehydrogenase in rat mitochondria." Archives of Biochemistry and Biophysics 259, no. 2 (December 1987): 412–22. http://dx.doi.org/10.1016/0003-9861(87)90507-8.

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36

Randall, Daniel C. "Eliminating Unnecessary Lactate Dehydrogenase Testing." Archives of Internal Medicine 157, no. 13 (July 14, 1997): 1441. http://dx.doi.org/10.1001/archinte.1997.00440340069006.

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37

Tajiri, J. "Lactate dehydrogenase isozyme and hypothyroidism." Archives of Internal Medicine 145, no. 10 (October 1, 1985): 1929b—1930. http://dx.doi.org/10.1001/archinte.145.10.1929b.

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38

Tajiri, Junichi. "Lactate Dehydrogenase Isozyme and Hypothyroidism." Archives of Internal Medicine 145, no. 10 (October 1, 1985): 1929. http://dx.doi.org/10.1001/archinte.1985.00360100203045.

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39

Ishikawa, Jinko, and Masato Maekawa. "Laboratory investigation of patients with high lactate dehydrogenase activity, by lactate dehydrogenase isozyme analysis." SEIBUTSU BUTSURI KAGAKU 51, no. 4 (2007): 243–46. http://dx.doi.org/10.2198/sbk.51.243.

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40

REIS, G. J., H. W. KAUFMAN, G. L. HOROWITZ, and R. C. PASTERNAK. "Usefullness of Lactate Dehydrogenase and Lactate Dehydrogenase Isoenzymes for Diagnosis of Acute Myocardial Infarction." Survey of Anesthesiology 32, no. 6 (December 1988): 365???373. http://dx.doi.org/10.1097/00132586-198812000-00006.

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41

Nicholson, Robin W. "Usefulness of lactate dehydrogenase and lactate dehydrogenase isoenzymes for diagnosis of acute myocardial infarction." Annals of Emergency Medicine 17, no. 8 (August 1988): 862. http://dx.doi.org/10.1016/s0196-0644(88)80576-6.

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42

Reis, Gregg J., Harvey W. Kaufman, Gary L. Horowitz, and Richard C. Pasternak. "Usefulness of lactate dehydrogenase and lactate dehydrogenase isoenzymes for diagnosis of acute myocardial infarction." American Journal of Cardiology 61, no. 10 (April 1988): 754–58. http://dx.doi.org/10.1016/0002-9149(88)91061-2.

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43

Nuwayhid, N. F., G. F. Johnson, and R. D. Feld. "Multipoint kinetic method for simultaneously measuring the combined concentrations of acetoacetate-beta-hydroxybutyrate and lactate-pyruvate." Clinical Chemistry 35, no. 7 (July 1, 1989): 1526–31. http://dx.doi.org/10.1093/clinchem/35.7.1526.

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Abstract This is a multipoint kinetic method for simultaneously determining acetoacetate (AcAc) plus beta-hydroxybutyrate and lactate plus pyruvate in a single cuvette of the Multistat III centrifugal analyzer. In the first step, AcAc and pyruvate are completely reduced, using 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) and lactate dehydrogenase (EC 1.1.1.27) in the presence of excess NADH at pH 7.5, to beta-hydroxybutyrate and lactate, respectively. After dilution, the endogenous beta-hydroxybutyrate and lactate and that resulting from reduction are simultaneously oxidized by their respective dehydrogenases in the presence of excess NAD+ at pH 9.0. Adjustment of the relative enzyme concentrations allows simultaneous estimation of AcAc plus beta-hydroxybutyrate and lactate plus pyruvate by analyzing multipoint absorbance data, collected during the oxidation reaction, with use of a two-component linear-regression model. Total run-to-run CVs were 6.4% and 6.1% at 5 mmol/L beta-hydroxybutyrate and 5 mmol/L lactate, respectively. The method was designed to be useful for identifying the cause of an increased anion gap in serum.

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44

Sato, Joji, Mamoru Wakayama, and Kazuyoshi Takagi. "Lactate Dehydrogenase Involved in Lactate Metabolism of Acetobacter Pasteurianus." Procedia Environmental Sciences 28 (2015): 67–71. http://dx.doi.org/10.1016/j.proenv.2015.07.010.

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45

Burlina, A., S. Secchiero, R. Bertorelle, M. Plebani, and M. Zaninotto. "Immunoglobulin A (lambda chains) conjugated with lactate dehydrogenase in serum." Clinical Chemistry 33, no. 6 (June 1, 1987): 1085–86. http://dx.doi.org/10.1093/clinchem/33.6.1085.

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Abstract An atypical pattern for lactate dehydrogenase (EC 1.1.1.27) isoenzymes in a patient with sclerosis of the bladder neck was ascribable to complexing between lactate dehydrogenase and IgA. This complex formation was also replicable "in vitro." We determined that the IgA bound to lactate dehydrogenase was of the lambda type, a very unusual occurrence.

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46

Bais, Renze, Allan M. Rofe, and Robert A. J. Conyers. "Inhibition of endogenous oxalate production: biochemical considerations of the roles of glycollate oxidase and lactate dehydrogenase." Clinical Science 76, no. 3 (March 1, 1989): 303–9. http://dx.doi.org/10.1042/cs0760303.

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1. Both the peroxisomal, flavin-linked glycollate oxidase [(S)-2-hydroxy-acid oxidase; EC 1.1.3.15] and the cytosolic, nicotinamide–adenine dinucleotide (NAD)-linked lactate dehydrogenase (l-lactate dehydrogenase; EC 1.1.1.27) are thought to contribute to the formation of oxalate from its immediate precursors, glycollate and glyoxylate, but the relative contributions of each enzyme to endogenous oxalate production is not known. 2. In rat liver homogenates, [14C]oxalate production from labelled glycollate is halved and that from labelled glyoxylate is increased fourfold by the addition of either NAD or NADH. 3. In isolated rat hepatocytes, the 3-hydroxy-1H-pyrrole-2,5-dione derivatives of glycollate, which are specific inhibitors of glycollate oxidase, have a greater effect on glycollate metabolism than on glyoxylate metabolism. 4. These findings are consistent with an important role for lactate dehydrogenase in oxalate formation from glyoxylate. 5. With human and rat liver homogenates and with purified human liver glycollate oxidase and rabbit muscle lactate dehydrogenase, dl-phenyl-lactate (2 mmol/l) completely inhibits glycollate oxidase but has no effect on lactate dehydrogenase. On the other hand, the reduced form of a chemically synthesized, NAD–pyruvate adduct (1 mmol/l) almost completely inhibited lactate dehydrogenase but had no effect on glycollate oxidase. 6. Either alone or in combination, dl-phenyl-lactate and reduced NAD–pyruvate adduct reduce oxalate production from glycollate and glyoxylate in isolated rat hepatocytes, but do not abolish it completely. 7. These findings support a role for another enzyme, probably glycollate dehydrogenase (EC 1.1.99.14), in oxalate production in integrated cell metabolism. 8. In relation to renal oxalate stone disease, these results suggest that the therapeutic inhibition of glycollate oxidase or lactate dehydrogenase would not completely prevent the endogenous formation of oxalate.

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47

Laganá, Giuseppina, Davide Barreca, Antonella Calderaro, and Ersilia Bellocco. "Lactate Dehydrogenase Inhibition: Biochemical Relevance and Therapeutical Potential." Current Medicinal Chemistry 26, no. 18 (September 2, 2019): 3242–52. http://dx.doi.org/10.2174/0929867324666170209103444.

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Lactate dehydrogenase (LHD) is a key enzyme of anaerobic metabolism in almost all living organisms and it is also a functional checkpoint for glucose restoration during gluconeogenesis and single-stranded DNA metabolism. This enzyme has a well preserved structure during evolution and among the species, with little, but sometimes very useful, changes in the amino acid sequence, which makes it an attractive target for the design and construction of functional molecules able to modulate its catalytic potential and expression. Research has focused mainly on the selection of modulator especially as far as LDH isozymes (especially LDH-5) and lactate dehydrogenases of Plasmodium falciparum (pfLDH) are concerned. This review summarizes the recent advances in the design and development of inhibitors, pointing out their specificity and therapeutic potentials.

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48

Rana, Faraz Ali, Helen Mary Robert, Madiha Ilyas, Asad Mahmood, Muhammad Amir, and Nabeela Khan. "DIAGNOSTIC UTILITY OF SERUM LACTATE DEHYDROGENASE LEVELS (LDL) IN DIFFERENTIATING MEGALOBLASTIC ANEMIA FROM MYELODYSPLASTIC SYNDROMES IN PAKISTAN." PAFMJ 71, no. 5 (October 30, 2021): 1539–43. http://dx.doi.org/10.51253/pafmj.v71i5.5003.

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Objective: To study the diagnostic utility of lactate dehydrogenase levels in differentiating megaloblastic anemia from myelodysplastic anemia in Pakistan. Study Design: Comparative cross-sectional study. Place and Duration of Study: Department of Hematology, Armed Forces Institute of Pathology, Rawalpindi, Pakistan from Feb, 2019 to Aug, 2019. Methodology: In this study, total 240 patients (18-75 years of age) males and females were selected by consecutive sampling technique and were equally divided into 3 groups; patients with megaloblastic anemia, patients with myelodysplastic syndromes and healthy control group. The clinical history and duration of anemia were recorded on special designed proforma. The laboratory investigations including lactate dehydrogenase levels were also noted. Both types of anemia were compared on basis of Lactate Dehydrogenase Levels. Results: The lactate dehydrogenase levels in megaloblastic group were more than 3000 IU/L in 58 out of 80 patients (72.5%). On other hand, myelodysplastic group had 79 out of 80 patients with lactic acid dehydrogenase levels below 450 IU/L (98.75%). The difference in lactic acid dehydrogenase levels between both groups was found to be statistically significant. Conclusion: Serum lactate dehydrogenase levels can be used to differentiate megaloblastic anemia from other anemia especially myelodysplastic syndromes before doing a bone marrow examination. High lactate dehydrogenase levels above 3000 IU/L in megaloblastic anemia can differentiate it from other anemia.

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49

Brooks, G. A., H. Dubouchaud, M. Brown, J. P. Sicurello, and C. E. Butz. "Role of mitochondrial lactate dehydrogenase and lactate oxidation in the intracellular lactate shuttle." Proceedings of the National Academy of Sciences 96, no. 3 (February 2, 1999): 1129–34. http://dx.doi.org/10.1073/pnas.96.3.1129.

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50

Sweetlove, L. J., R. Dunford, R. G. Ratcliffe, and N. J. Kruger. "Lactate metabolism in potato tubers deficient in lactate dehydrogenase activity." Plant, Cell & Environment 23, no. 8 (August 2000): 873–81. http://dx.doi.org/10.1046/j.1365-3040.2000.00605.x.

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