Bibliografias temáticas / Lactate dehydrogenase

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Literatura científica selecionada sobre o tema "Lactate dehydrogenase"

Autor: Grafiati
Publicado: 4 de junho de 2021
Última modificação: 25 de julho de 2025

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Artigos de revistas sobre o assunto "Lactate dehydrogenase"

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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 (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, indepe
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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 (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.
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Oren, Aharon, and Peter Gurevich. "Diversity of lactate metabolism in halophilic archaea." Canadian Journal of Microbiology 41, no. 3 (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 cons
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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 (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 r
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Anand, Usha. "Lactate Dehydrogenase." Clinical Chemistry 59, no. 3 (2013): 585. http://dx.doi.org/10.1373/clinchem.2011.178541.

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

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

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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 (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 involve
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Teses / dissertações sobre o assunto "Lactate dehydrogenase"

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Shu, Hun-Chi. "D-lactid acid analysis using sequential injection analysis and amperometric biosensor." Lund : Dept. of Biotechnology, Lund University, 1994. http://catalog.hathitrust.org/api/volumes/oclc/38950881.html.

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Nobbs, Timothy J. "Protein engineering of E. coli malate dehydrogenase and B. stearothermophilus lactate dehydrogenase." Thesis, Open University, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.293546.

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Dempster, Sally. "Lactate dehydrogenase : studies towards the design, synthesis and co-crystallisation of bisubstrate inhibitors." Thesis, University of Nottingham, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.594762.

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Christopher, Mary Elizabeth. "Characterization of hypoxically induced lactate dehydrogenase in maize." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq22968.pdf.

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Higham, Christopher W. "A study of lactate dehydrogenase from Plasmodium falciparum." Thesis, University of Bristol, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.299529.

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Diez-Aguirre, Jesus Javier. "A cold-active lactate dehydrogenase from an Antarctic bacterium." Thesis, Imperial College London, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.312140.

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Haghayegh, Jahromi Neda, and Gheinani Ali Hashemi. "RNA Silencing of Lactate Dehydrogenase Gene in Rhizopus oryzae." Thesis, Högskolan i Borås, Institutionen Ingenjörshögskolan, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:hb:diva-20404.

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RNA silencing with direct delivery of siRNA has been used to suppress ldhA gene expression in filamentous fungus Rhizopus oryzae. Here, for the first time we show that, introducing small interfering RNA which consequently forms silencing complexes can alter the gene expression and we report a significant reduction of lactic acid production for isolates containing short (25 nt) synthetic siRNA. In all samples lactic acid production was reduced comparing with wild types. The average concentration of lactic acid production by Rhizopus oryzae during batch fermentation process where glucose has bee
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Lomas, Andrew Philip. "Towards a small molecule inhibitor of Lactate Dehydrogenase-A." Thesis, University of Oxford, 2011. http://ora.ox.ac.uk/objects/uuid:d7f1416e-0d3d-4b4e-af62-7bbf4d52cf90.

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Lactate Dehydrogenase-A (LDH-A) is up-regulated in a broad array of cancers and is associated with poor prognosis. Involved in the hypoxic response, LDH-A is a HIF-1 target and is responsible for the enzymatic reduction of pyruvate to lactate. This is important for several reasons, chiefly (1) the regeneration of NAD+ which feeds back into earlier glycolytic stages and (2) the depletion of intracellular pyruvate concentrations. High intracellular pyruvate is known to inhibit HDACs and is associated with increased apoptosis. LDH-A is also known to be controlled by oncogenes such as c-Myc sugges
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Silcock, Alan J. "Enantioselective synthesis and cyclisation studies of 2-hydroxy esters." Thesis, University of Bristol, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.299530.

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Shoemark, Deborah Karen. "The kinetic characterization of the lactate dehydrogenase enzyme from Plasmodium falciparum." Thesis, University of Bristol, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.326677.

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Livros sobre o assunto "Lactate dehydrogenase"

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Boyce, Julian. Lactate dehydrogenase isoenzymes in malignant serous effusions. The Author], 1989.

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2

Beaudoin, Marc. Glucose, lactate and lactate dehydrogenase levels in the human kidney carcinoma cell line A498 (ATCC HTB-44). Laurentian University, 1993.

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3

Mulholland, Peter. M-subunit lactate dehydrogenase in aspirated fluids from benign and malignant lesions. The Author], 1988.

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4

Ostojic, Sandra. A study of the Michaelis constant for the H4 and M4 isoenzymes of lactate dehydrogenase. Laurentian University, 1994.

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5

Muldoon, Lori. Glucose, lactate, and lactate dehydrogenase activity of the small cell lung cancer line H-209 and the drug resistant variant H-209/V6. Laurentian University, 1992.

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6

Hickey, Rosemary. A Chemical inhibition method for lactate dehydrogenase isoenzyme 1: An application for the investigation of response to MACOP-B chemotherapy. The Author], 1991.

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7

Jarmoluk, Petra. Laktat- und Katecholaminbestimmungen als Mittel zur Leistungssteuerung im Judo: Eine empirische Langzeitstudie an Weltklasseathletinnen. SFT-Verlag, 1989.

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8

Lee, R. J. Lactic acid metabolism and lactate dehydrogenases of Vibrio species. Portsmouth Polytechnic,School of Pharmacy..., 1987.

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9

Schäfer, Heinz-Günter. Synthese von Holo-Dehydrogenasen durch kovalente Fixierung eines NAD⁺-Analogen [NAD-Analogen] an Lactat- und Alkohol-Dehydrogenase zum Aufbau von Enzymreaktoren. [s.n.], 1985.

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10

Sada, Nagisa, and Tsuyoshi Inoue. Lactate Dehydrogenase. Edited by Detlev Boison. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190497996.003.0029.

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Glucose is transported into neurons and used as an energy source. It is also transported into astrocytes, a type of glial cell, and converted to lactate, which is then released to neurons and used as another energy source. The latter is called the astrocyte-neuron lactate shuttle. Although the lactate shuttle is a metabolic pathway, it also plays important roles in neuronal activities and brain functions. We recently reported that this metabolic pathway is involved in the antiepileptic effects of the ketogenic diet. Lactate dehydrogenase (LDH) is a metabolic enzyme that mediates the lactate sh
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Capítulos de livros sobre o assunto "Lactate dehydrogenase"

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Davis, James W., Dana Forman, La Scienya M. Jackson, et al. "Lactate Dehydrogenase." In Encyclopedia of Intensive Care Medicine. Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-00418-6_1814.

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Schomburg, Dietmar, and Dörte Stephan. "L-Lactate dehydrogenase." In Enzyme Handbook 9. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-85200-8_27.

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Schomburg, Dietmar, and Dörte Stephan. "D-Lactate dehydrogenase." In Enzyme Handbook 9. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-85200-8_28.

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Kline, E. S., R. B. Brandt, J. E. Laux, and S. E. Spainhour. "Mitochondrial Lactate Dehydrogenase." In Integration of Mitochondrial Function. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2551-0_32.

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Stapenhorst França, Fernanda, Ivi Juliana Bristot, and Fábio Klamt. "LDHA (Lactate Dehydrogenase A)." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101640.

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Kamp, Marc Willem. "Lactate Dehydrogenase – Computational Studies." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_236.

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Schomburg, Dietmar, and Dörte Stephan. "L-Lactate dehydrogenase (cytochrome)." In Enzyme Handbook 10. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-57756-7_96.

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Schomburg, Dietmar, and Dörte Stephan. "D-Lactate dehydrogenase (cytochrome)." In Enzyme Handbook 10. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-57756-7_97.

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Stapenhorst França, Fernanda, Ivi Juliana Bristot, and Fábio Klamt. "LDHA (Lactate Dehydrogenase A)." In Encyclopedia of Signaling Molecules. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101640-1.

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Engin, Yasemin Zeynep, Kemal Turhan, Aslı Yazağan, and Asım Örem. "Mortality Prediction with Lactate and Lactate Dehydrogenase." In Bioinformatics and Biomedical Engineering. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16483-0_8.

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Trabalhos de conferências sobre o assunto "Lactate dehydrogenase"

1

Uchayash, Sajid, Sunney Que, Md Fazlay Rubby, and Long Que. "A Nanostructure-Electrode-Based Electrochemical Sensor for Detection of Lactate Dehydrogenase." In 2024 IEEE Nanotechnology Materials and Devices Conference (NMDC). IEEE, 2024. https://doi.org/10.1109/nmdc58214.2024.10894011.

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Taertulakarn, Somchat, Adisorn Tuantranont, Pussadee Tobanluepop, and Chuchart Pintavirooj. "The preliminary study of lactate detection based on lactate dehydrogenase/nictotinamide adenine dinucleotide." In 2012 5th Biomedical Engineering International Conference (BMEiCON). IEEE, 2012. http://dx.doi.org/10.1109/bmeicon.2012.6465514.

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Hoyer, Nils, Michael Brun Andersen, Lene Collatz, Emilia Kassandra Achilles Åttingsberg, and Saher Burhan Shaker. "Lactate dehydrogenase predicts disease progression in patients with IPF." In ERS International Congress 2023 abstracts. European Respiratory Society, 2023. http://dx.doi.org/10.1183/13993003.congress-2023.pa1143.

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Serganova, Inna, Asif Rizwan, Xiaohui Ni, Sunitha Thakur, Ronald Blasberg, and Jason Koutcher. "Abstract 1003: A link between lactate dehydrogenase A, lactate and tumor phenotype identified by imaging." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1003.

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Manea, Laur. "LACTATE DEHYDROGENASE ENZYME AND ITS IMPLICATIONS IN CHEMICAL STRESS SITUATIONS." In 17th International Multidisciplinary Scientific GeoConference SGEM2017. Stef92 Technology, 2017. http://dx.doi.org/10.5593/sgem2017/61/s25.102.

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Dahanayake, Thinesh, Karoline Moon, Katie Smolnycki, et al. "Lactate Dehydrogenase 5 Expression is Increased In Idiopathic Pulmonary Fibrosis." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a3503.

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Eid, H., A. El Kik, A. Riachy, et al. "Lactate dehydrogenase (LDH) reinforcement in predicting Covid-19 patient’s outcomes." In ERS International Congress 2022 abstracts. European Respiratory Society, 2022. http://dx.doi.org/10.1183/13993003.congress-2022.3132.

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Braca, A., M. De Leo, L. Peruzzi, et al. "Inhibitors of lactate dehydrogenase (hLDH5) from Polygala flavescens subsp. flavescens." In GA 2017 – Book of Abstracts. Georg Thieme Verlag KG, 2017. http://dx.doi.org/10.1055/s-0037-1608078.

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Bi, Aiwei, Jun Xu, Nan Jin, et al. "Abstract 3737: Mutant isocitrate dehydrogenase driven metabolic reprogramming results in therapeutic vulnerability to lactate dehydrogenase inhibition." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-3737.

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Anuradh Gunawardena, Sandun D Fernando, and Dwaine A Braasch. "Performance analysis of a bio fuel cell based on Lactate Dehydrogenase." In 2008 Providence, Rhode Island, June 29 - July 2, 2008. American Society of Agricultural and Biological Engineers, 2008. http://dx.doi.org/10.13031/2013.25166.

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Relatórios de organizações sobre o assunto "Lactate dehydrogenase"

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Ma, Lianjia. Multichannel Simultaneous Determination of Activities of Lactate Dehydrogenase. Office of Scientific and Technical Information (OSTI), 2000. http://dx.doi.org/10.2172/764689.

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Piper, Robert C. Parasite Lactate Dehydrogenase for Diagnosis of Plasmodium Falciparum. Phase II. Defense Technical Information Center, 1997. http://dx.doi.org/10.21236/adb230017.

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Li, Fenglei. Automated High Throughput Protein Crystallization Screening at Nanoliter Scale and Protein Structural Study on Lactate Dehydrogenase. Office of Scientific and Technical Information (OSTI), 2006. http://dx.doi.org/10.2172/892735.

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Viksna, Ludmila, Oksana Kolesova, Aleksandrs Kolesovs, Ieva Vanaga, and Seda Arutjunana. Clinical characteristics of COVID-19 patients (Latvia, Spring 2020). Rīga Stradiņš University, 2020. http://dx.doi.org/10.25143/fk2/hnmlhh.

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Data include following variables: Demographics, epidemiological history, comorbidities, diagnosis, complications, and symptoms on admission to the hospital. Also, body’s temperature and SpO2. Blood cells: white cells count (WBC), neutrophils (Neu), lymphocytes (Ly), eosinophils (Eo) and monocytes (Mo), percentages of segmented and banded neutrophils, erythrocytes (RBC), platelet count (PLT), hemoglobin (Hb), and hematocrit (HCT); Inflammatory indicators: erythrocyte sedimentation rate (ESR) and C-reactive protein (CRP); Tissue damage indicators: alanine aminotransferase (ALT), lactate dehydrog
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Tengamnuay, Parkpoom, Achariya Sailasuta, and Garnpimol C. Ritthidej. Efficacy and mechanistic studies of chitosan as nasal absorption enhancer of peptide drugs. Chulalongkorn University, 1998. https://doi.org/10.58837/chula.res.1998.21.

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Objective: To evaluate the safety and efficacy of chitosan (CS) as nasal absorption enhances of peptides. Methods: Two types of chitosans, i.e. CS J (free amine chitosan) and CD G (water-soluble glutamate salt), were evaluate for their masal absorption enhancing effectd on L-Tyr-D-Arg([D-Arg[square]]-Kyotorphic), an enzymatically stable dipeptide, using an in situ rat nasal perfusion technique. The two chitosans were subsequently studies for their possible membrane damaging effects based on measurements of releases mucosal components and histological evaluation. Results: At 0.5% w/v, both CS J
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