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Relevant bibliographies by topics / Lactate dehydrogenase

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Academic literature on the topic 'Lactate dehydrogenase'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 March 2023

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Journal articles on the topic "Lactate dehydrogenase"

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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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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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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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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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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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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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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Dissertations / Theses on the topic "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 been used as a sole carbon source, diminished from 2.06 g/l in wild types to 0.36 g/l in knockdown samples which signify 5.7 times decrease. Interestingly, the average concentration of ethanol production was increased from 0.38 g/l in wild types to 0.45 g/l in knockdown samples. In some samples we were able to report even a 10 fold decrease in lactic acid production. Since R.oryzae is capable to assimilate a wide range of carbohydrates hydrolysed from lignocellulosic material in order to produce many economically valuable bulk material such as ethanol, these results suggest that RNA silencing is a useful method for industrial biotechnology to be applied in fungus Rhizopus oryzae in order to trigger the metabolism and gene expression toward a desired product.

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8

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 suggesting an oncogenic role. Studies have shown that the knock-out of LDH-A reduces proliferation and tumourgenicity, and stimulates the mitochondria. This thesis therefore had three aims: firstly, to validate LDH-A inhibition and elucidate its full nature in terms of the implications for tumour survival; secondly, to ascertain the role of LDH-B in order to determine whether selectivity towards LDH-A would be a necessary feature of any small molecule; lastly, to recapitulate siRNA mediated LDH-A inhibition with small molecule inhibitors that had the potential for clinical application. The thesis examined both clinical data and a broad panel of cultured cancer cell types in order to select appropriate model in which to validate siRNA mediated inhibition of LDH-A and LDH-B. After it was demonstrated that LDH-A inhibition reduced the growth of cultured cells, a range of techniques were used to quantify this reduced growth in terms of cell death and changes in metabolism. Further to this, literature studies had proposed a role for LDH-B in maintaining lactate fuelled tumour growth; however, this thesis shows that in the cell lines studied, lactate-fuelled tumour growth was an LDH-A dependent phenomenon. Finally, a high throughput assay system was designed and validated and a library of small molecules was selected, synthesized, and screened in order to identify selective inhibitors of LDH-A.

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9

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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Books on the topic "Lactate dehydrogenase"

1

Boyce, Julian. Lactate dehydrogenase isoenzymes in malignant serous effusions. [s.l: 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). Sudbury, Ont: Laurentian University, 1993.

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3

Mulholland, Peter. M-subunit lactate dehydrogenase in aspirated fluids from benign and malignant lesions. [s.l: 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. Sudbury, Ont: 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. Sudbury, Ont: 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. [S.l: The Author], 1991.

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7

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

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8

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

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9

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 shuttle, and its inhibition hyperpolarizes neurons and suppresses seizures. This enzyme is also a molecular target of stiripentol, a clinically used antiepileptic drug for Dravet syndrome. This review provides an overview of electrical regulation by the astrocyte-neuron lactate shuttle, and then introduces LDH as a metabolic target against epilepsy.

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10

Rani, Reshma. Lactate Dehydrogenase: Biochemistry, Function and Clinical Significance. Nova Science Publishers, Incorporated, 2019.

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Book chapters on the topic "Lactate dehydrogenase"

1

Davis, James W., Dana Forman, La Scienya M. Jackson, James W. Davis, Javier Garau, David N. O’Dwyer, Elisa Vedes, et al. "Lactate Dehydrogenase." In Encyclopedia of Intensive Care Medicine, 1317. Berlin, Heidelberg: 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, 157–64. Berlin, Heidelberg: 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, 165–69. Berlin, Heidelberg: 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, 349–56. Boston, MA: 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, 2835–39. Cham: 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, 1225–26. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_236.

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7

Schomburg, Dietmar, and Dörte Stephan. "L-Lactate dehydrogenase (cytochrome)." In Enzyme Handbook 10, 345–49. Berlin, Heidelberg: 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, 350–53. Berlin, Heidelberg: 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, 1–4. New York, NY: 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, 78–84. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16483-0_8.

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Conference papers on the topic "Lactate dehydrogenase"

1

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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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, Hao Dong Xu, Richard P. Phipps, Patricia J. Sime, and Matthew Kottmann. "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, E. Mekhael, K. Hoyek, N. Nassim, G. Khayat, G. Sleilaty, and M. Riachy. "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, C. Granchi, T. Tuccinardi, F. Minutolo, and N. De Tommasi. "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, Xiaojing Lan, Shuai Tang, Matthew Shou, Jia Liu, 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. St. Joseph, MI: American Society of Agricultural and Biological Engineers, 2008. http://dx.doi.org/10.13031/2013.25166.

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Jelassi, W., N. Abid, M. Loukil Ben Ali, N. Gader, M. Ben Ali, I. Chaabane, K. Bouzaidi, and H. Ghrairi. "Lactate dehydrogenase level: A predictive marker for severe COVID-19 infection." In ERS International Congress 2022 abstracts. European Respiratory Society, 2022. http://dx.doi.org/10.1183/13993003.congress-2022.3866.

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Cianci, Roberta, Ludovica Capitelli, Miriam Buonincontro, Rosalba Donizzetti, Dario Cuomo, Antonio Prisco, Francesco Squillante, and Vincenzo Bocchino. "Correlation between lactate dehydrogenase and therapeutic strategy in Covid-19 pneumonia." In ERS International Congress 2021 abstracts. European Respiratory Society, 2021. http://dx.doi.org/10.1183/13993003.congress-2021.pa1091.

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Reports on the topic "Lactate dehydrogenase"

1

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

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2

Piper, Robert C. Parasite Lactate Dehydrogenase for Diagnosis of Plasmodium Falciparum. Phase II. Fort Belvoir, VA: Defense Technical Information Center, April 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), August 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, December 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 dehydrogenase (LDH), and troponin T (TnT); Electrolytes: potassium and sodium concentration; Renal function indicators: creatinine and glomerular filtration rate (GFR); Coagulation tests: D-dimer, prothrombin time, and prothrombin index on admission to the hospital.

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