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    Wyświetlanie 1-10 z 10
    Tytuł:
    Kinetics and specificity of guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase towards substituted benzaldehydes.
    Autorzy:
    Panoutsopoulos, Georgios
    Beedham, Christine
    Powiązania:
    https://bibliotekanauki.pl/articles/1041542.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    xanthine oxidase
    dopamine
    benzaldehydes
    aldehyde oxidase
    protocatechuic aldehyde
    isovanillin
    Opis:
    Molybdenum-containing enzymes, aldehyde oxidase and xanthine oxidase, are important in the oxidation of N-heterocyclic xenobiotics. However, the role of these enzymes in the oxidation of drug-derived aldehydes has not been established. The present investigation describes the interaction of eleven structurally related benzaldehydes with guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase, since they have similar substrate specificity to human molybdenum hydroxylases. The compounds under test included mono-hydroxy and mono-methoxy benzaldehydes as well as 3,4-dihydroxy-, 3-hydroxy-4-methoxy-, 4-hydroxy-3-methoxy-, and 3,4-dimethoxy-benzaldehydes. In addition, various amines and catechols were tested with the molybdenum hydroxylases as inhibitors of benzaldehyde oxidation. The kinetic constants have shown that hydroxy-, and methoxy-benzaldehydes are excellent substrates for aldehyde oxidase (Km values 5×10-6 M to 1×10-5 M) with lower affinities for xanthine oxidase (Km values around 10-4 M). Therefore, aldehyde oxidase activity may be a significant factor in the oxidation of the aromatic aldehydes generated from amines and alkyl benzenes during drug metabolism. Compounds with a 3-methoxy group showed relatively high Vmax values with aldehyde oxidase, whereas the presence of a 3-hydroxy group resulted in minimal Vmax values or no reaction. In addition, amines acted as weak inhibitors, whereas catechols had a more pronounced inhibitory effect on the aldehyde oxidase activity. It is therefore possible that aldehyde oxidase may be critical in the oxidation of the analogous phenylacetaldehydes derived from dopamine and noradrenaline.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 3; 649-663
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Is aldehyde dehydrogenase inhibited by sulfur compounds? In vitro and in vivo studies
    Autorzy:
    Iciek, Małgorzata
    Górny, Magdalena
    Bilska-Wilkosz, Anna
    Kowalczyk-Pachel, Danuta
    Powiązania:
    https://bibliotekanauki.pl/articles/1038534.pdf
    Data publikacji:
    2018
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    aldehyde dehydrogenase
    reactive sulfur species
    sulfane sulfur
    Opis:
    Aldehyde dehydrogenase (ALDH) catalyzes the critical step of ethanol metabolism, i.e. transformation of toxic acetaldehyde to acetic acid. It is a redox sensitive protein with the key Cys in its active site. Recently, it has been documented that activity of some proteins can be modified by sulfur-containing molecules called reactive sulfur species leading to the formation of hydro- persulfides. The aim of the present study was to examine whether ALDH activity can be modified in this way. Studies were performed in vitro using yeast ALDH and various reactive sulfur species, including Na2S, GSSH, K2Sx, Na2S2O3, and garlic-derived allyl sulfides. The effect of garlic-derived trisulfide on ALDH activity was also studied in vivo in the rat liver. The obtained results clearly demonstrated that ALDH could be regulated by sulfur species which inhibited its enzymatic activity. The results also suggested that not H2S but polysulfides or hydropersulfides were the oxidizing species responsible for this modification. This process was easily reversible by reducing agents. After the treatment with polysulfides or hydropersulfides the level of protein-bound sulfur increased, while the activity of the enzyme dramatically decreased. Moreover, the study demonstrated that ALDH activity was inhibited in vivo in the rat liver after garlic-derived trisulfide administration. This is the first study reporting the regulation of ALDH activity by sulfane sulfur species and the results suggest that it leads to the inhibition of the enzyme.
    Źródło:
    Acta Biochimica Polonica; 2018, 65, 1; 125-132
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Synthesis and biological activity of some various aldehyde and 1,2,3-triazole containing heterocyclic compounds
    Autorzy:
    Narigara, Rajesh
    Joshi, Deepkumar
    Bhola, Yogesh
    Jani, Gaurang
    Powiązania:
    https://bibliotekanauki.pl/articles/1070887.pdf
    Data publikacji:
    2019
    Wydawca:
    Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
    Tematy:
    Azides
    Hydrazones
    aldehyde
    anti-fungal
    antibacterial
    triazoles
    Opis:
    As heterocyclic compounds show good biological activity, we have synthesized nitrogen containing compounds among them 6b, 6d, 8a and 8b have shown very good antimicrobial activity with remarkable inhibition zones N'-(anthracen-9-ylmethylene)-5-methyl-1-phenyl-1H-1,2,3-triazole-4 carbohydrazide and N'-(3-(benzyloxy)benzylidene)-5-methyl-1-phenyl-1H-1,2,3-triazole-4-carbohydrazide (6a-d, 8a-d) was synthesized from various aldehyde and 5-methyl-1-phenyl-1H-1,2,3-triazole-4-carbohydrazide by condensation in acidic media. All intermediates and final compounds were confirmed by 1H-NMR, 13C-NMR, Mass Spectroscopy methods and IR analysis.
    Źródło:
    World Scientific News; 2019, 123; 246-257
    2392-2192
    Pojawia się w:
    World Scientific News
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    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:
    Enzymatic oxidation of phthalazine with guinea pig liver aldehyde oxidase and liver slices: inhibition by isovanillin
    Autorzy:
    Panoutsopoulos, Georgios
    Beedham, Christine
    Powiązania:
    https://bibliotekanauki.pl/articles/1041506.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    xanthine oxidase
    phthalazine
    aldehyde oxidase
    liver slices
    disulfiram
    isovanillin
    allopurinol
    Opis:
    The enzymes aldehyde oxidase and xanthine oxidase catalyze the oxidation of a wide range of N-heterocycles and aldehydes. These enzymes are widely known for their role in the metabolism of N-heterocyclic xenobiotics where they provide a protective barrier by aiding in the detoxification of ingested nitrogen-containing heterocycles. Isovanillin has been shown to inhibit the metabolism of aromatic aldehydes by aldehyde oxidase, but its inhibition towards the heterocyclic compounds has not been studied. The present investigation examines the oxidation of phthalazine in the absence and in the presence of the inhibitor isovanillin by partially purified aldehyde oxidase from guinea pig liver. In addition, the interaction of phthalazine with freshly prepared guinea pig liver slices, both in the absence and presence of specific inhibitors of several liver oxidizing enzymes, was investigated. Aldehyde oxidase rapidly converted phthalazine into 1-phthalazinone, which was completely inhibited in the presence of isovanillin (a specific inhibitor of aldehyde oxidase). In freshly prepared liver slices, phthalazine was also rapidly converted to 1-phthalazinone. The formation of 1-phthalazinone was completely inhibited by isovanillin, whereas disulfiram (a specific inhibitor of aldehyde dehydrogenase) only inhibited 1-phthalazinone formation by 24% and allopurinol (a specific inhibitor of xanthine oxidase) had little effect. Therefore, isovanillin has been proved as an inhibitor of the metabolism of heterocyclic substrates, such as phthalazine, by guinea pig liver aldehyde oxidase, since it had not been tested before. Thus it would appear from the inhibitor results that aldehyde oxidase is the predominant enzyme in the oxidation of phthalazine to 1-phthalazinone in freshly prepared guinea pig liver slices, whereas xanthine oxidase only contributes to a small extent and aldehyde dehydrogenase does not take any part.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 4; 943-951
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Salivary aldehyde dehydrogenase - temporal and population variability, correlations with drinking and smoking habits and activity towards aldehydes contained in food
    Autorzy:
    Giebułtowicz, Joanna
    Dziadek, Marta
    Wroczyński, Piotr
    Woźnicka, Katarzyna
    Wojno, Barbara
    Pietrzak, Monika
    Wierzchowski, Jacek
    Powiązania:
    https://bibliotekanauki.pl/articles/1040385.pdf
    Data publikacji:
    2010
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    superoxide dismutase
    fluorescence
    aldehyde dehydrogenase
    aldehydes
    nutrition safety
    saliva
    salivary peroxidase
    Opis:
    Fluorimetric method based on oxidation of the fluorogenic 6-methoxy-2-naphthaldehyde was applied to evaluate temporal and population variability of the specific activity of salivary aldehyde dehydrogenase (ALDH) and the degree of its inactivation in healthy human population. Analyzed was also its dependence on drinking and smoking habits, coffee consumption, and its sensitivity to N-acetylcysteine. Both the specific activity of salivary ALDH and the degree of its inactivation were highly variable during the day, with the highest activities recorded in the morning hours. The activities were also highly variable both intra- and interpersonally, and negatively correlated with age, and this correlation was stronger for the subgroup of volunteers declaring abstinence from alcohol and tobacco. Moderately positive correlations of salivary ALDH specific activity with alcohol consumption and tobacco smoking were also recorded (rs ~0.27; p=0.004 and rs =0.30; p=0.001, respectively). Moderate coffee consumption correlated positively with the inactivation of salivary ALDH, particularly in the subgroup of non-drinking and non-smoking volunteers. It was found that mechanical stimulation of the saliva flow increases the specific activity of salivary ALDH. The specific activity of the salivary ALDH was strongly and positively correlated with that of superoxide dismutase, and somewhat less with salivary peroxidase. The antioxidant-containing drug N-acetylcysteine increased activity of salivary ALDH presumably by preventing its inactivation in the oral cavity. Some food-related aldehydes, mainly cinnamic aldehyde and anisaldehyde, were excellent substrates of the salivary ALDH3A1 enzyme, while alkenals, particularly those with short chain, were characterized by lower affinity towards this enzyme but high catalytic constants. The protective role of salivary ALDH against aldehydes in food and those found in the cigarette smoke is discussed, as well as its participation in diminishing the effects of alcohol- and smoking-related oxidative stress.
    Źródło:
    Acta Biochimica Polonica; 2010, 57, 3; 361-368
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Biochemical characteristics of AtFAR2, a fatty acid reductase from Arabidopsis thaliana that reduces fatty acyl-CoA and -ACP substrates into fatty alcohols
    Autorzy:
    Doan, Thuy
    Carlsson, Anders
    Stymne, Sten
    Hofvander, Per
    Powiązania:
    https://bibliotekanauki.pl/articles/1038782.pdf
    Data publikacji:
    2016
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Arabidopsis thaliana
    chloroplast
    fatty acyl-CoA/ACP reductase
    fatty alcohol
    fatty aldehyde
    Opis:
    Fatty alcohols and derivatives are important for proper deposition of a functional pollen wall. Mutations in specific genes encoding fatty acid reductases (FAR) responsible for fatty alcohol production cause abnormal development of pollen. A disrupted AtFAR2 (MS2) gene in Arabidopsis thaliana results in pollen developing an abnormal exine layer and a reduced fertility phenotype. AtFAR2 has been shown to be targeted to chloroplasts and in a purified form to be specific for acyl-ACP substrates. Here, we present data on the in vitro and in planta characterizations of AtFAR2 from A. thaliana and show that this enzyme has the ability to use both, C16:0-ACP and C16:0-CoA, as substrates to produce C16:0-alcohol. Our results further show that AtFAR2 is highly similar in properties and substrate specificity to AtFAR6 for which in vitro data has been published, and which is also a chloroplast localized enzyme. This suggests that although AtFAR2 is the major enzyme responsible for exine layer functionality, AtFAR6 might provide functional redundancy to AtFAR2.
    Źródło:
    Acta Biochimica Polonica; 2016, 63, 3; 565-570
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Cyanopyrans: Synthesis and antimicrobial screening
    Autorzy:
    Baluja, Shipra
    Moteriya, Pooja
    Chanda, Sumitra
    Nandha, Kajal
    Powiązania:
    https://bibliotekanauki.pl/articles/1192682.pdf
    Data publikacji:
    2016
    Wydawca:
    Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
    Tematy:
    N-dimethylformamide
    pyrazolo aldehyde
    cyanopyran
    antimicrobial activity
    agar-well diffusion method
    N
    Opis:
    A series of cyanopyran derivatives have been synthesized and their structures were confirmed by IR, 1H NMR and mass spectral data. All these synthesized compounds were tested in vitro for their antimicrobial potential by agar-well diffusion method against Gram positive, Gram negative strains of bacteria as well as fungal strains in N,N-dimethylformamide and dimethyl sulfoxide.
    Źródło:
    World Scientific News; 2016, 46; 36-51
    2392-2192
    Pojawia się w:
    World Scientific News
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Sex propheromone of the pine tree lappet moth Dendrolimus pini and its use in attractant-based monitoring system
    Autorzy:
    Grodner, J.
    Zander, R.
    Powiązania:
    https://bibliotekanauki.pl/articles/55011.pdf
    Data publikacji:
    2010
    Wydawca:
    Sieć Badawcza Łukasiewicz - Instytut Przemysłu Organicznego
    Tematy:
    cross-coupling reaction
    stereoselective reduction
    acetal
    aldehyde
    attractant
    Lepidoptera
    Lasiocampidae
    Pinus sylvestris
    field experiment
    Scotch pine
    sex pheromone
    pine tree
    lappet moth
    Dendrolimus pini
    attractant-based monitoring system
    needle
    forest
    Polska
    monitoring
    insecticide
    plant protection
    Opis:
    The study presents a new strategy of synthesis of the pine-tree lappet moth sex pheromone via hydrolysis of the (5Z,7E)-1,1-diethoxy-5,7-dodecadiene (propheromone) and their using in biological tests with pheromone traps. The field trials showed that a sticky delta traps with propheromone at dose of 2.4 mg was the most suitable for monitoring of the population of the pine tree lappet moth.
    Źródło:
    Pestycydy; 2010, 1-4
    0208-8703
    Pojawia się w:
    Pestycydy
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    SAFETY OF LABOUR IN SPIRIT PRODUCTION
    BEZPIECZNA EKSPLOATACJA PRODUKCJI WYROBÓW ALKOHOLOWYCH
    БЕЗОПАСНОЕ ПРОИЗВОДСТВО АЛКОГОЛЬНЫХ ПРОДУКТОВ
    Autorzy:
    Zochshuk, Vitaliy
    Powiązania:
    https://bibliotekanauki.pl/articles/576876.pdf
    Data publikacji:
    2016-12-30
    Wydawca:
    Międzynarodowy Instytut Innowacji Nauka – Edukacja – Rozwój w Warszawie
    Tematy:
    ethyl alcohol, BROKD, BRUBAK-1, BRUBAK-2, Shpaniv spirit plant, vapours of ethanol, ethanol water, a vapours of aldehyde, nitrogen dioxide, carbon dioxide
    alkohol etylowy, BROKD, BRUBAK-1, BRUBAK-2, gorzelnia Shpanovsky, pary etanolu, etanol i woda, opary aldehydu, dwutlenek azotu, dwutlenek węgla
    этиловый спирт, БРУКД, БРУВАК-1, БРУВАК-2, Шпановский спиртзавод, пары этилового спирта, этанол вода, пары альдегида, диоксид азота, углекислый газ
    Opis:
    W tym artykule przedstawione zostały ogólne zasady produkcji alkoholu etylowego. Opisano potencjalne niebezpieczne zagrożenia tej produkcji. Omawiany schemat technologiczny produkcyji alkoholu etylowego przedstawiono na przykładzie gorzelni Shpanovsky. Wskazano na szczególne zagrożenia i szkodliwe czynniki produkcji. Wyjaśniono wpływ zagrożeń chemicznych na organizm człowieka. Przedstawiono środki ochrony osobistej oraz poprawy procesów głównego wyposażenia technologicznego w oparciu o analizę zdarzających się wypadków w pracy. Podano zalecenia dotyczące użytkowania urządzeń technologicznych.
    In this article general principles of the manufacturing of alcohol are presented. Existed dangerous hazards are described. The considered technological scheme of production of alcohol on the example of Shpaniv alcohol plant are offered. It is described specific threat and harmful production factors. It is stressed the impact of chemical hazards on the human body. Proposed personal protective equipment based on potential accidents in the process of operation and repair of the main technological equipment. Developed recommendations on use of technological equipment.
    В данной статье рассмотрено общие принципы изготовления спирта. Наведены опасные общие опасные факторы. Рассмотрено технологическая схема производства спирта на примере Шпановского завода. Описаны конкретные опасные и вредные производственные факторы. Описано влияние химических вредных факторов на организм человека. Предложены индивидуальные средства защиты на основе возможных аварийных ситуаций в процессе эксплуатации и ремонта основного технологического оборудования. Разработаны рекомендации по эксплуатации технологического оборудования.
    Źródło:
    International Journal of New Economics and Social Sciences; 2016, 4(2); 154-161
    2450-2146
    2451-1064
    Pojawia się w:
    International Journal of New Economics and Social Sciences
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-10 z 10

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