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    Wyświetlanie 1-7 z 7
    Tytuł:
    The activity of class I, II, III and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in the sera of bladder cancer patients
    Autorzy:
    Orywal, Karolina
    Jelski, Wojciech
    Werel, Tadeusz
    Szmitkowski, Maciej
    Powiązania:
    https://bibliotekanauki.pl/articles/1038688.pdf
    Data publikacji:
    2017
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    alcohol dehydrogenase isoenzymes
    aldehyde dehydrogenase
    bladder cancer
    Opis:
    Objectives. Studies on alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) activity in the sera of patients with malignant neoplasms show that cancer cells in many organs may release ADH isoenzymes into the blood. The aim of this study was to investigate the differences in the activity of ADH isoenzymes and ALDH in the sera of patients with bladder cancer (BCa), and with different grades of the disease. Material and Methods. Blood samples were taken from 39 patients with BCa (15 patients with low-grade and 24 with high-grade BCa) and from 60 healthy subjects. Class III and IV of ADH and total ADH activity were measured using the photometric method, while class I and II ADH and ALDH activity using the fluorometric method with class-specific fluorogenic substrates. Results. The activity of the class I ADH isoenzyme and total ADH was significantly higher in the sera of BCa patients as compared to control group. Analysis of ALDH activity did not show statistically significant differences between the tested groups. Significantly higher total activity of ADH in comparison to control was found in both, low-grade and high-grade BCa group. The activity of ADH class I was also significantly higher in high-grade BCa group when compared to low-grade patients and controls. Conclusion. The increase of total ADH activity in the sera of BCa patients seems to be caused by isoenzymes released from cancerous cells. The higher activity of ADH I probably resulted from metastatic tumors as significant increase was detected only in the sera of high-grade bladder cancer patients.
    Źródło:
    Acta Biochimica Polonica; 2017, 64, 1; 81-84
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    The alcohol dehydrogenase isoenzyme (ADH IV) as a candidate tumour marker of esophageal cancer
    Autorzy:
    Jelski, Wojciech
    Laniewska-Dunaj, Magdalena
    Niklinski, Jacek
    Kozłowski, Miroslaw
    Laudanski, Jerzy
    Szmitkowski, Maciej
    Powiązania:
    https://bibliotekanauki.pl/articles/1039560.pdf
    Data publikacji:
    2013
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    alcohol dehydrogenase isoenzymes
    esophageal cancer
    Opis:
    Objective: Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are present in esophageal cancer cells. Moreover the total activity of ADH as well as the activity of class IV ADH isoenzyme is significantly higher in cancer tissue than in healthy mucosa. The activity of these enzymes in cancer cells is reflected in the sera and could thus be helpful for diagnostics of esophageal cancer. The aim of this study was to investigate a potential significance of ADH isoenzymes and ALDH as tumour markers of esophageal cancer. We defined diagnostic sensitivity, specificity, predictive value for positive and negative results, and receiver-operating characteristics (ROC) curve for tested enzymes. Methods: Serum samples were taken for routine biochemical investigation from 180 patients with esophageal cancer before treatment. Total ADH activity was measured by a photometric method with p-nitrosodimethylaniline as a substrate and ALDH activity by a fluorometric method with 6-methoxy-2-naphtaldehyde as a substrate. For the measurement of the activity of class I and II isoenzymes we employed the fluorometric methods, with class-specific fluorogenic substrates. The activity of class III alcohol dehydrogenase was measured by a photometric method with formaldehyde and class IV with m-nitrobenzaldehyde as a substrate. Results: There was a significant increase in the activity of class IV of ADH isoenzyme (7.65 mU/l vs 5.88 mU/l) and total ADH activity (1198 mU/l vs 848 mU/l) in the sera of esophageal cancer patients compared to the control. The diagnostic sensitivity for ADH IV was 72%, the specificity 76%, the positive and negative predictive values were 80% and 72% respectively. The area under the ROC curve for ADH IV was 0.65. Conclusion: The results suggest a potential significance of ADH IV as a marker of esophageal cancer.
    Źródło:
    Acta Biochimica Polonica; 2013, 60, 3; 489-493
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Natural stereospecific hydrogen isotope transfer in alcohol dehydrogenase-catalysed reduction
    Autorzy:
    Zhang, B.
    Pionnier, S.
    Powiązania:
    https://bibliotekanauki.pl/articles/146970.pdf
    Data publikacji:
    2002
    Wydawca:
    Instytut Chemii i Techniki Jądrowej
    Tematy:
    alcohol dehydrogenase
    chiral isotopomers
    deuterium
    isotope tracing
    Opis:
    The enantiomeric purity of natural alfa-monodeuterated enantiomers, (R) and (S) ethanol-1-d1, in the alcohol produced by sugar fermentation with yeast was studied by 2H NMR using their esters derived from optical mandelic acid. The results of isotope tracing experiments show that the transfer pathways of the two enantiotopic hydrogens of the methylene group are different. It was observed that (S)-deuterium comes only from the medium water. The (R)-deuterium transfered by NADH in alcohol dehydrogenase reduction of the acetaldehyde is of complex origin. Some of them originates from carbon bound hydrogen of the sugar, especially from C(4) position of glucose and most of them comes from water. Only a small portion of the NADH deuterium is incorporated indirectly from water through enzyme catalysed exchange between the pro-S site of NADH and flavin. When a carbonyl compound (ethyl acetoacetate) was reduced under the same conditions during the alcoholic fermentation, among the NADH-transfered deuterium, only a small portion comes from water while most comes from the unexchangeable positions of the glucose.
    Źródło:
    Nukleonika; 2002, 47,suppl.1; 29-31
    0029-5922
    1508-5791
    Pojawia się w:
    Nukleonika
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Dehydrogenazy alkoholowe pochodzenia mikrobiologicznego : właściwości i ich zastosowanie
    Microbial alcohol dehydrogenases : properties and their application
    Autorzy:
    Szczepańska, E.
    Boratyński, F.
    Powiązania:
    https://bibliotekanauki.pl/articles/172286.pdf
    Data publikacji:
    2014
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    dehydrogenaza alkoholowa
    biotransformacja
    bakterie
    alcohol dehydrogenase
    biotransformations
    bacteria
    Opis:
    Biotransformations involve mainly microorganisms or individual enzymes applied to catalyze chemical reactions [1]. This field of science is particularly important, because it allows to obtain optically active compounds, which are valuable raw materials for pharmaceutical (Fig. 3, Fig. 6, Fig. 20, Fig. 21), wood and paper (Fig. 18), food (Fig. 4), textile (Fig. 12), cosmetic (Fig. 14) industries and environmental protection (Fig. 19). Oxidoreductases, in particular alcohol dehydrogenases (E.C.1.1.1.1, ADH) are valuable biocatalysts enabling to obtain enantiomerically pure products. These enzymes, commonly found in nature, catalyze both oxidation and reduction reactions [3]. Described dehydrogenases descend from mesophilic, psychrophilic and thermophilic microorganisms. The increasing application of thermophiles is due to their exceptional resistance against heat and organic solvents. The article describes and explains how microbial ADH’s interact with NAD+/NADH or NADP+/NADPH and present those enzymes which catalyze reactions with both forms of cofactors. The alcohol dehydrogenases from yeast are particularly commonly used [9–14]. Bacterial enzymes, among them ADH isolated from Thermoanaerobacter brockii [47–51], are widely distributed too. In addition, the literature describes a number of (R)-specific ADH’s from Lactobacillus kefir [40–42], L. brevis [45, 46], Leisofonia sp. [20] Pseudomonas fluorescens [23] and (S)- -specific ADH’s from Rhodococcus erythropolis [15, 16], Thermus sp. [30], Sulfolobus solfataricus [23, 28] and many others.
    Źródło:
    Wiadomości Chemiczne; 2014, 68, 11-12; 1049-1071
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Yeast metabolic adaptation to environment
    Autorzy:
    Drygaś, Barbara
    Biesiadecka, Magdalena Karolina
    Powiązania:
    https://bibliotekanauki.pl/articles/1181238.pdf
    Data publikacji:
    2017
    Wydawca:
    Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
    Tematy:
    adaptation
    alcohol dehydrogenase
    quorum-sensing substance
    yeast metabolism
    Opis:
    Yeast metabolism has been a subject of research since the XIX century, when Louis Pasteur had proved that yeast are live organisms and fermentation is one of the processes to produce molecular energy. Yeast ability to ferment is a consequence of alcohol dehydrogenase (ADH) activity, the group of enzymes responsible for sugar conversion in to ethanol as ADH1, and alcohol metabolism as a source of carbohydrates (ADH2). The group of ADH enzymes play a crucial role for yeast adaptation especially in rich sugar environments such as after angiosperm occurrence. Evolution of yeast genes is based on chromosomal multiplication event, previously explained as a Whole Genome Duplication (WGD), presently it has been proven that the yeast common ancestor is a hybrid from different strains. Duplication cause that some multiplaies genes accumulate mutation without cell growth burden and consequently favor formations exploiting new features of proteins. Yeast ability to ferment make them dominate in a sugar environment, however Saccharomyces cerevisiae evolve some quorum-sensing mechanism, which plays crucial role in population messengers as tyrosol which is signaling about cellular density in culture. Moreover there are scientific reports about yeast specific social-wraps which suggest that yeast surviving depends on more complex mechanisms, which pose challenges for researchers. The aim of this article is a short review of yeast metabolic strategy which allow yeast to dominate in high sugar environments and abilities which make yeast so important in nature.
    Źródło:
    World Scientific News; 2017, 72; 558-564
    2392-2192
    Pojawia się w:
    World Scientific News
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Enancjoselektywna enzymatyczna desymetryzacja katalizowana oksydoreduktazami. Dehydrogenazy w reakcji redukcji. Część I
    Enantioselective enzymatic desymmetrization catalyzed by oxidoreductases. Dehydrogenases in reduction reactions. Part I
    Autorzy:
    Kołodziejska, R.
    Karczmarska-Wódzka, A.
    Tafelska-Kaczmarek, A.
    Studzińska, R.
    Wróblewski, M.
    Augustyńska, B.
    Powiązania:
    https://bibliotekanauki.pl/articles/171686.pdf
    Data publikacji:
    2014
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    redukcja asymetryczna
    dehydrogenaza alkoholowa
    kofaktor
    asymmetric reduction
    alcohol dehydrogenase
    cofactor
    Opis:
    Enzymes act as biocatalysts whether are also mediating in all anabolic and catabolic pathways, playing an extremely important role in the cells of all life forms. Catalytic potential of oxidoreductases is most commonly used in reduction reactions. Dehydrogenases and reductases catalyze the reversible desymmetrization reactions of meso and prochiral carbonyl compounds and alkenes. The oxidoreductase- catalyzed reactions require cofactors to initiate catalysis. In most cases, it is nicotinamide adenine dinucleotide (NADH) or its phosphorylated derivative (NADPH), which acts as a hydride donor. The necessity of employing expensive cofactors was, for the long time, one of the main limitations to the use of dehydrogenases. This problem was solved by developing a regeneration system of a cofactor in the reaction environment. Various systems are used for the cofactor recycling. In the case of a carbonyl compound reduction, an irreversible oxidation of formic acid to carbon dioxide is most frequently used. In this paper, selected examples of whole-cell and isolated enzymes applications in the carbonyl compound reduction are discussed. The application of baker’s yeast, microorganisms and dehydrogenases in enantioselective enzymatic desymmetrization (EED) of prochiral ketones leads to a broad spectrum of chiral alcohols used as intermediates in the syntheses of many pharmaceuticals and compounds presenting a potential biological activity.
    Źródło:
    Wiadomości Chemiczne; 2014, 68, 9-10; 763-782
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Differential responses of aquatic and aerobic forms of Echinochloa crus-galli (L.) Beauv. and E. colona (L.) Link. by morpho-physiological and molecular analysis
    Autorzy:
    Khedr, A.-H.A.
    Serag, M.M.
    Shaaban, H.E.
    Abogadallah, G.M.
    Powiązania:
    https://bibliotekanauki.pl/articles/9989.pdf
    Data publikacji:
    2017
    Wydawca:
    Fundacja na Rzecz Młodych Naukowców
    Tematy:
    alcohol dehydrogenase
    ADH zob.alcohol dehydrogenase
    aquatic form
    aerobic form
    Echinochloa crus-galli
    Echinochloa colona
    habitat alteration
    morphophysiological analysis
    molecular analysis
    phosphoenolopyruvate carboxylase
    Rubisco
    Opis:
    Echinochloa crus-galli and E. colona are serious weeds around the world. Morphological and biochemical features of aquatic and aerobic forms of both species were investigated experimentally by transplanting the seedlings reciprocally between water-saturated and aerobic soils (70% field capacity). When the plants were grown in water-saturated soil, a significant decrease in tiller height was observed in E. crus-galli, but not in E. colona. Upon growing the plants in aerobic soil, internode length and spike dry weight increased significantly in E. crus-galli, but decreased significantly in E. colona. Growth under aerobic condition caused a significant increase in PEPC/Rubisco ratio, but a significant decrease was observed under water-saturated conditions. When E. crus-galli was transplanted in aerobic soil, several forms of peroxidase were upregulated. Contrarily, in E. colona peroxidase isoforms did not respond to habitat change. Gene expression of ADH in E. colona was constitutive at a fairly high level under native habitats then enhanced with reversing habitat that caused anoxic and mild drought conditions. Both species tend to grow faster under aerobic conditions by modifying the photosynthetic machinery and capacity of scavenging of reactive oxygen species. Furthermore, ADH appears to play a role in supporting growth under water-saturated conditions.
    Źródło:
    Environment, Earth and Ecology; 2017, 1, 1
    2543-9774
    2451-4225
    Pojawia się w:
    Environment, Earth and Ecology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-7 z 7

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