Lactate dehydrogenase Dotaz Zobrazit nápovědu
The inter- and intraspecies variability of lactate dehydrogenase (ldh) gene was determined among the predominant ruminal lactate utilizing bacteria. Nearly complete nucleotide sequences of ldh gene, encoding NAD-dependent lactate dehydrogenase of three Megasphaera elsdenii and six Selenomonas ruminantium strains, were obtained and compared. Phylogenetic analyses revealed a limited variability between the ldh sequences studied. The majority of differences observed were silent mutations at the 3rd position of codons. Surprisingly, the intraspecies diversity of the ldh gene among S. ruminantium isolates was higher than the interspecies level between S. ruminantium and M. elsdenii, which strongly suggests the possibility of acquisition of this gene by horizontal gene transfer.
- MeSH
- bachor mikrobiologie MeSH
- bakteriální proteiny genetika MeSH
- bodová mutace MeSH
- DNA bakterií chemie genetika MeSH
- fylogeneze MeSH
- genetická variace * MeSH
- kyselina mléčná metabolismus MeSH
- L-laktátdehydrogenasa genetika MeSH
- Megasphaera enzymologie genetika izolace a purifikace metabolismus MeSH
- molekulární sekvence - údaje MeSH
- sekvenční analýza DNA MeSH
- sekvenční homologie MeSH
- Selenomonas enzymologie genetika izolace a purifikace metabolismus MeSH
- shluková analýza MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bakteriální proteiny MeSH
- DNA bakterií MeSH
- kyselina mléčná MeSH
- L-laktátdehydrogenasa MeSH
Lactate dehydrogenase (LDH, E.C. 1.1.1.27) activity was studied in an experimental model (the liver bile of cholecystectomized patients and of rats) by electrophoretic separation on agar gel. The prevalence of the liver LDH5 isoenzyme in bile obtained in this manner is the proof that this fraction is secreted by the liver. The experimental conclusions are supported by the author's own clinical observations of prevalence of the cathodic isocomponents LDH4 and LDH5 in serum, as an indicator of cholestasis in conditions characterized by bile duct obstruction.
- MeSH
- cholestáza enzymologie MeSH
- izoenzymy MeSH
- játra enzymologie MeSH
- krysa rodu Rattus MeSH
- L-laktátdehydrogenasa metabolismus MeSH
- lidé MeSH
- žlučník enzymologie MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- izoenzymy MeSH
- L-laktátdehydrogenasa MeSH
- MeSH
- antigeny virové imunologie MeSH
- dospělí MeSH
- imunologické techniky * MeSH
- LDH virus imunologie MeSH
- lidé středního věku MeSH
- lidé MeSH
- oční nemoci imunologie MeSH
- senioři MeSH
- test inhibice adherence leukocytů * MeSH
- Check Tag
- dospělí MeSH
- lidé středního věku MeSH
- lidé MeSH
- mužské pohlaví MeSH
- senioři MeSH
- ženské pohlaví MeSH
- Publikační typ
- anglický abstrakt MeSH
- časopisecké články MeSH
- Názvy látek
- antigeny virové MeSH
The method of enzyme-electrophoresis in agar gel according to Wieme (1959) was used for the study of lactate dehydrogenase (LDH) and malate dehydrogenase (MDH) isoenzymes of 24-hour and 48-hour Salmonella cultures exposed to a 0.02% solution of potassium dichloroisocyanurate (PDIC). Severe repression of LDH and MDH isoenzymes was observed immediately after the exposure of the culture to the disinfectant solution. A significant decrease in the content of the isoenzyme LDH1 and of the cytoplasmic fraction (C1) of MDH simultaneously with the appearance of the fractions LDH4, LDH1a and LDH1b were established in the strains cultured on MPA in the course of 24 hours following the exposure. A tendency to a decrease in the LDH1 content was preserved in the experimental cultures after 48 hours, but the spectrum of MDH isoenzymes showed almost no differences in comparison with that of MDH isoenzymes in 48-hour cultures of the control strains.
- MeSH
- časové faktory MeSH
- dezinficiencia farmakologie MeSH
- izoenzymy metabolismus MeSH
- L-laktátdehydrogenasa metabolismus MeSH
- malátdehydrogenasa metabolismus MeSH
- Salmonella enzymologie MeSH
- triaziny farmakologie MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- dezinficiencia MeSH
- izoenzymy MeSH
- L-laktátdehydrogenasa MeSH
- malátdehydrogenasa MeSH
- triaziny MeSH
Lactate dehydrogenase (LDH) and malate dehydrogenase (MDH) electrophoretic tissue patterns of two different orders of Elasmobranchii: Carchariniformes (Galeus melanostomus and Prionace glauca) and Squaliformes (Etmopterus spinax and Scymnorinus licha) were studied. The number of loci expressed for these enzymes was the same of other elasmobranch species. Differences in tissue distribution were noted in LDH from G. melanostomus due to the presence of an additional heterotetramer in the eye tissue. There were also differences in MDH. In fact, all the tissues of E. spinax and G. melanostomus showed two mitochondrial bands. Major differences were noted in the number of isozymes detected in the four compared elasmobranchs. The highest polymorphism was observed in E. spinax and G. melanostomus, two species that live in changeable environmental conditions. The resistance of isozymes after urea treatment was examined; the resulting patterns showed a quite good resistance of the enzymes, higher for LDH than MDH, also at urea concentration much greater than physiological one. These results indicated that the total isozyme resistance can be considered higher in urea accumulators (such as elasmobranchs) than in the non-accumulators (such as teleosts).
- MeSH
- denaturace proteinů MeSH
- Elasmobranchii metabolismus MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- fylogeneze MeSH
- fyziologická adaptace * MeSH
- izoenzymy metabolismus MeSH
- játra enzymologie MeSH
- konformace proteinů MeSH
- L-laktátdehydrogenasa chemie metabolismus MeSH
- malátdehydrogenasa chemie metabolismus MeSH
- močovina chemie metabolismus MeSH
- molekulární evoluce MeSH
- mozek enzymologie MeSH
- myokard enzymologie MeSH
- oči enzymologie MeSH
- rybí proteiny chemie metabolismus MeSH
- svaly metabolismus MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- srovnávací studie MeSH
- Názvy látek
- izoenzymy MeSH
- L-laktátdehydrogenasa MeSH
- malátdehydrogenasa MeSH
- močovina MeSH
- rybí proteiny MeSH
The impact of environmental pollution at the place of residence of pregnant women and of their smoking habits on the cellular energy metabolism of placental tissue was investigated. Samples of full-term placentas were randomly collected from two environmentally different regions of Slovakia (Bratislava, Stará Lubovna) and the activity of lactate dehydrogenase (LDH) was measured. Our results showed enhanced LDH activity in the placenta that was dependent on both the type of environmental pollutants at the place of residence and the smoking habits during pregnancy. The enhanced LDH activity may reflect hypoxic conditions due to the accumulation of heavy metals and toxic compounds of tobacco smoke in the placental tissue. A high content of heavy metal particles, found in placental samples from Stará Lubovna in our previous studies, might contribute to the increased LDH activity in placentas from this region. We hypothesize that fine metal particles deposited in the placental tissue might be phagocytozed by the syncytiotrophoblast, thus contributing to the decreased oxygen level in placental tissue.
- MeSH
- kouření MeSH
- L-laktátdehydrogenasa metabolismus MeSH
- látky znečišťující životní prostředí analýza farmakologie MeSH
- lidé MeSH
- placenta chemie účinky léků enzymologie MeSH
- těhotenství MeSH
- těžké kovy analýza MeSH
- Check Tag
- lidé MeSH
- těhotenství MeSH
- ženské pohlaví MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Geografické názvy
- Slovenská republika MeSH
- Názvy látek
- L-laktátdehydrogenasa MeSH
- látky znečišťující životní prostředí MeSH
- těžké kovy MeSH
Lactate dehydrogenase (LDH, EC 1.1.1.27) was isolated in 86% purity from carp (Cyprinus carpio) hepatopancreas using agarose T-gel (mercaptoethanol bound to agarose via divinylsulphone) affinity chromatography medium and Iontosorb phenyl hydrophobic chromatography medium. Gel filtration chromatography of the LDH obtained shows molecular weight to be 26,900 Da.
- MeSH
- játra enzymologie MeSH
- kapři MeSH
- kosterní svaly enzymologie MeSH
- králíci MeSH
- kur domácí MeSH
- L-laktátdehydrogenasa izolace a purifikace MeSH
- myokard enzymologie MeSH
- pankreas enzymologie MeSH
- zvířata MeSH
- Check Tag
- králíci MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- L-laktátdehydrogenasa MeSH
OBJECTIVE: An anaerobic type of glycolysis exemplified by hyperproduction of the lactate dehydrogenase (LDH) subunit M has been detected in lung tumours, while a similar pattern has been found in concomitant pleural effusions (PE). The aim of this study was to verify the presence of the LDH subunit M in PEs of different aetiology and to compare its expression with markers of inflammation. MATERIAL AND METHODS: LDH isoenzymes were estimated and the LDH5/LDH1 coefficient was calculated in paraneoplastic PEs (n = 99), including subgroups with a different tumour ultrastructure, origin and pleural involvement. The expression pattern was compared with parainflammatory PEs (n = 21), transudates (n = 16) and with the expression of 13 inflammatory markers in PEs. RESULTS: The LDH5/LDH1 coefficient was higher in PEs associated with non-small-cell lung cancer (NSCLC) and with pleura-invading tumours, and lower in PEs of small-cell lung cancer and tumours without a confirmed pleural involvement. The LDH5/LDH1 coefficient positively correlated with uPA, IL-8, IL-10, sICAM, sVCAM, MPO and MMP-9. CONCLUSIONS: In accordance with inflammatory markers, it appears that the expression of LDH and its isoenzymes in PEs reflects the host reaction in pleural space and, in NSCLC, may also feature the anaerobic phenotype of cancer cells.
- MeSH
- biologické markery metabolismus MeSH
- izoenzymy krev metabolismus MeSH
- L-laktátdehydrogenasa krev metabolismus MeSH
- laktátdehydrogenasa 5 MeSH
- lidé středního věku MeSH
- lidé MeSH
- mediátory zánětu analýza MeSH
- metastázy nádorů MeSH
- nádory plic enzymologie patologie ultrastruktura MeSH
- pleurální výpotek enzymologie etiologie MeSH
- podjednotky proteinů krev metabolismus MeSH
- Check Tag
- lidé středního věku MeSH
- lidé MeSH
- mužské pohlaví MeSH
- ženské pohlaví MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- biologické markery MeSH
- izoenzymy MeSH
- L-laktátdehydrogenasa MeSH
- lactate dehydrogenase 1 MeSH Prohlížeč
- laktátdehydrogenasa 5 MeSH
- mediátory zánětu MeSH
- podjednotky proteinů MeSH
Serum lactate dehydrogenase (LD) patterns of 16 calves with total artificial heart (TAH) were studied to identify a mean LD pattern in their serum (survival 51-293 days). Evaluations were made by the sum of vectors method (SV). The mean LD pattern was determined from serum LD patterns, interval days of 33 - 49 with TAH. Serum LD patterns of control and mean LD pattern differed significantly (n = 12, P < 0.05) in single isoenzymes and resultant vectors as the representatives of LD patterns. The different tissues with an increased risk of being affected were identified by evaluation of LD patterns in the serum of calves within term without perceptible acute damage and in the terminal stage of experiments. Such identified organs suggest that the organism under study is out of balance and specific treatment is needed.
Lactate dehydrogenase (LDH) activity and its isoenzymatic fractions were measured in bone marrow blood and in peripheral venous blood from 16 haematologically normal subjects. Total LDH activity was significantly higher in marrow than in venous blood (428.8 +/- 98.4 vs 260.1 +/- 40.2 mU/l, p < 0.0001). The same was true for the absolute values of its isoenzymatic fractions. The percentage fractions LDH 1 and LDH 5 were similar in the two regions, while LDH 3 and LDH 4 were higher in medullary blood (p < 0.05) and LDH 2 was higher in peripheral blood (p < 0.05). The Spearman test showed a limited correlation between marrow and peripheral total LDH activity values (p < 0.05). This seems to be at least in part sustained by the highly significant correlations existing in LDH 3 and LDH 4 values, reported to be pre-eminent isoforms in maturing haematopoietic cells (p < 0.005 and p < 0.001, respectively). These findings could be attributed to an apoptotic regulation of marrow cell production.
- MeSH
- dospělí MeSH
- izoenzymy MeSH
- kostní dřeň enzymologie MeSH
- L-laktátdehydrogenasa krev metabolismus MeSH
- lidé středního věku MeSH
- lidé MeSH
- referenční hodnoty MeSH
- Check Tag
- dospělí MeSH
- lidé středního věku MeSH
- lidé MeSH
- mužské pohlaví MeSH
- ženské pohlaví MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- izoenzymy MeSH
- L-laktátdehydrogenasa MeSH