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Artigos de revistas sobre o tema "Lactate dehydrogenase"

Autor: Grafiati

Publicado: 4 de junho de 2021

Última modificação: 25 de julho de 2025

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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 (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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2

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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3

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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4

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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5

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

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6

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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7

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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8

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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9

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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10

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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11

Hua, Yibo, Chao Liang, Jundong Zhu, et al. "Expression of lactate dehydrogenase C correlates with poor prognosis in renal cell carcinoma." Tumor Biology 39, no. 3 (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 wer

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12

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 (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 chromat

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13

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 (1989): 4076–81. http://dx.doi.org/10.1016/s0021-9258(19)84964-5.

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14

Chen, P.-P., S.-M. Tsai, H.-M. Wang, et al. "Lactate dehydrogenase isoenzyme patterns in auricular pseudocyst fluid." Journal of Laryngology & Otology 127, no. 5 (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

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15

Deck, Lorraine M., Robert E. Royer, Brian B. Chamblee, et al. "Selective Inhibitors of Human Lactate Dehydrogenases and Lactate Dehydrogenase from the Malarial ParasitePlasmodiumfalciparum." Journal of Medicinal Chemistry 41, no. 20 (1998): 3879–87. http://dx.doi.org/10.1021/jm980334n.

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16

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

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17

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

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18

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

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19

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

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20

Wiwanitkit, V. "Interesting Lactate dehydrogenase Isoenzymes." Chulalongkorn Medical Journal 45, no. 10 (2001): 855–63. http://dx.doi.org/10.58837/chula.cmj.45.10.2.

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21

Raghuwanshi, Kapil, Bhupesh Kushram, Dileep Dandotiya, Sudhakar Petkar, Swapnali Tambade, and Mahendra Gandhe. "Lactate dehydrogenase (LDH) as an indicator of pre-eclampsia." Bioinformation 21, no. 2 (2025): 116–20. https://doi.org/10.6026/973206300210116.

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High blood pressure (higher than 140/90 mm Hg), proteinuria and swelling due to fluid retention are symptoms of preeclampsia, a disease that affects pregnant women after the 20th week of pregnancy. The cytoplasm of cells undergoing anaerobic glycolysis contains the enzyme lactate dehydrogenase or LDH. Therefore, it is of interest to ascertain the blood lactate dehydrogenase levels of pre-eclamptic women, to assess and analyze these levels, to compare lactate dehydrogenase levels in different groups of preeclampsia patients and healthy controls, and to examine the role of lactate dehydrogenase

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22

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 (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

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23

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 (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 respecti

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24

P.S., Rajani,. "Effects of Ancylostoma ceylanicum Infection on Lactate Dehydrogenase Activity in Tissues of Mesocricetus auratus." Asian Journal of Research in Zoology 7, no. 4 (2024): 89–95. http://dx.doi.org/10.9734/ajriz/2024/v7i4173.

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Aim: The present research aims to study the effects of Ancylostoma ceylanicum infection on lactate dehydrogenase activity in the tissues of Mesocricetus auratus. Methodology: In the current investigation, Ancylostoma ceylanicum, a hookworm was infected in the host, a hamster Mesocricetus auratus experimentally in laboratory conditions in Hyderabad from 1992 to 1996. The infected host was then studied using the parameters of Lactate dehydrogenase activity in various tissues. The Lactate Dehydrogenase content in M. auratus was investigated biochemically in both the infected and control samples.

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25

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 (1985): 1920. http://dx.doi.org/10.1093/clinchem/31.11.1920.

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26

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 (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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27

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 (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

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28

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 (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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29

Khitam Abdul Wahhab Ali, Abeer Anwer Ahmed, and Suhad Taha Mohammed. "Determination of Serum Myeloperoxidase (MPO) and lactate dehydrogenase (LDH) as a tumour Marker in Chronic Myeloid Leukaemia (CML)." Journal of the Pakistan Medical Association 74, no. 10 (Supple-08) (2024): S283—S286. http://dx.doi.org/10.47391/jpma-bagh-16-64.

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Objective: To evaluate the efficacy of serum myeloperoxidase and lactate dehydrogenase levels as tumour markers in chronic myeloid leukaemia patients after one-year treatment with tyrosine kinase inhibitors.Method: The case-control study was conducted at the College of Medicine, Mustansiriyah University, Baghdad, Iraq, in collaboration with the National Centre of Haematology, Baghdad, from December 2019 to April 2020. The cases comprised chronic myeloid leukaemia patients aged greater than or equal to18 years who had completed one-year treatment with tyrosine kinase inhibitor. They were divide

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30

Bernard, William V., and Thomas J. Divers. "Variations in serum sorbitol dehydrogenase, aspartate transaminase, and isoenzyme 5 of lactate dehydrogenase activities in horses given carbon tetrachloride." American Journal of Veterinary Research 50, no. 5 (1989): 622–23. https://doi.org/10.2460/ajvr.1989.50.05.622.

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SUMMARY Seven horses were given 0.5 mg of carbon tetrachloride/kg of body weight via a nasogastric tube. Subsequent hepatocellular damage was monitored by serum enzyme determinations of sorbitol dehydrogenase, isoenzyme 5 of lactate dehydrogenase, and aspartate transaminase activities. Creatinine kinase activity was evaluated as an indicator of muscle cell damage. Sorbitol dehydrogenase, isoenzyme 5 of lactate dehydrogenase, and aspartate transaminase activities were significanlty (P < 0.05) increased by 24 hours after carbon tetrachloride administration. Isoenzyme 5 of lactate dehydrogenas

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31

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 (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 eithe

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32

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 (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 myelodyspla

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33

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 (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 c

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34

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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35

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

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36

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

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37

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

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38

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

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39

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

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40

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

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41

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

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42

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

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43

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

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44

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 (1987): 412–22. http://dx.doi.org/10.1016/0003-9861(87)90507-8.

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45

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

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46

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

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47

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

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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 (1988): 365???373. http://dx.doi.org/10.1097/00132586-198812000-00006.

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