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  • 1
    Electronic Resource
    Electronic Resource
    Presence of epoxide hydrolase and glutathione S-transferase in human pulmonary alveolar macrophages (1988)
    Springer
    European journal of clinical pharmacology 34 (1988), S. 419-421 
    Details
    ISSN: 1432-1041
    Keywords: epoxide hydrolase ; glutathione S-transferase ; pulmonary macrophages ; bronchoalveolar lavage ; smokers/non-smokers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary Pulmonary alveolar macrophages (PAMs) were obtained from 11 patients by bronchoalveolar lavage. Epoxide hydrolase and glutathione S-transferase in sonicated PAMs were measured using benzo(a)pyrene-4,5-oxide as the substrate. The activity of epoxide hydrolase was 0.24±0.10 nmol/min/mg protein (mean±SD), and of glutathione S-transferase 0.22±0.12 nmol/min/mg protein. There was a significant difference in enzyme activities in the PAMs from smokers and non-smokers. Epoxides may be metabolized in PAMs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00542447
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  • 2
    Electronic Resource
    Electronic Resource
    Plasma protein binding of furosemide in the elderly (1987)
    Springer
    European journal of clinical pharmacology 32 (1987), S. 199-202 
    Details
    ISSN: 1432-1041
    Keywords: furosemide ; plasma protein binding ; old age ; youth
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary The protein binding of furosemide was investigated in plasma from 22 old and 11 young subjects by equilibrium dialysis. The unbound fraction of furosemide was 3.16% in plasma from the elderly and 1.71% in plasma from the young. A significant correlation was found between the unbound fraction of furosemide and the plasma concentration of albumin. The average number of binding sites was 3.8 (elderly) and 2.7 (young) 10−6 mol/g albumin. The average association constant (K) was 4.3 (elderly) and 4.2 (young) 105 M−1. By increasing the concentration of furosemide up to 200 µg/ml buffer the unbound fraction of the drug rose to 5.2% (elderly) and 3.5% (young).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00542196
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  • 3
    Electronic Resource
    Electronic Resource
    Hydroxylation of dibutylnitrosamine in the human liver and intestinal microsomal fractions (1986)
    Springer
    Archives of toxicology 58 (1986), S. 196-198 
    Details
    ISSN: 1432-0738
    Keywords: Dibutylnitrosamine ; Metabolism ; Human ; Rat ; Liver ; intestine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The metabolism of the bladder carcinogen N-nitroso-di-n-butylamine (NDBA) was studied in microsomal preparations of tissues of patients of both sexes, aged 59–69 years undergoing abdominal surgery. Samples of liver, ileum, and colon were of normal histological appearance. For comparison, samples of rat liver and small intestinal mucosa microsomes were included in the study. Using 1-14C-labeled NDBA, the biotransformation to hydroxylation products retaining the nitroso group, NDBA-2-OH, NDBA-3-OH, and NDBA-4-OH, respectively, was investigated by reversed phase HPLC. In order to separate these metabolites, pooled samples were analysed by normal phase HPLC. The rate of hydroxylation of NDBA was found to be 5.5 times higher in rat liver microsomes compared to those from human liver (2.86±0.29 vs 0.52±0.03 nM x min−1 x mg−1). NDBA-3-OH proved to be the major metabolite formed (〉80% of total metabolites). The metabolism of NDBA was low but detectable in seven out of nine specimens of human gut, 0.1–0.5 nM x mg−1 in 1 h of incubation, and of the same order of magnitude in rat intestinal tissue (0.4–0.6 nM x mg−1).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00340981
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  • 4
    Electronic Resource
    Electronic Resource
    Cytosolic epoxide hydrolase in humans: development and tissue distribution (1988)
    Springer
    Archives of toxicology 62 (1988), S. 254-257 
    Details
    ISSN: 1432-0738
    Keywords: Cytosolic epoxide hydrolase ; Humans ; Fetuses ; Adult subjects
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Cytosolic epoxide hydrolase activity was measured towards trans-stilbene oxide in 41 human adult livers, in 40 fetal livers, in 17 placentas and in fetal and adult lungs, kidneys and gut. The cytosolic epoxide hydrolase activity was measurable in all specimens investigated. The rate of formation of trans-stilbene glycol (pmol/min per mg protein, mean±SD) was 55.2±89.6 (fetal liver). 303.2±73.2 (adult liver) and 18.8±13.1 (placenta) In the fetal extrahepatic tissues, the cytosolic epoxide hydrolase activity was 70.0±9.4 (adrenals), 47.6±7.2 (gut), 69.4±22.5 (kidneys) and 43.2±19.2 (lungs) pmol/min per mg protein, whereas in the adult tissues it was 131.2±63.1 (kidneys), 27.8±20.3 (intestine), 8.5±2.8 (lungs) and 7.2±4.2 (urinary bladder) pmol/min per mg protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00332483
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  • 5
    Electronic Resource
    Electronic Resource
    Valpromide is a poor inhibitor of the cytosolic epoxide hydrolase (1989)
    Springer
    Archives of toxicology 63 (1989), S. 157-159 
    Details
    ISSN: 1432-0738
    Keywords: Cytosolic epoxide hydrolase ; Valpromide ; Liver ; Adult subjects and fetuses
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The effect of the antiepileptics valpromide and sodium valproate on the cytosolic epoxide hydrolase was studied in human fetal liver, kidneys and adrenals and from human adult liver and kidneys. Trans-stilbene oxide was used as substrate. Valpromide (10 mM) lowered the activity of the epoxide hydrolase to one half of the control in all organs studied. Sodium valproate (10 mM) was less powerful as an inhibitor than valpromide; however, it exerted a significant inhibition in all tissues studied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00316440
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  • 6
    Electronic Resource
    Electronic Resource
    Profile of drug metabolizing enzymes in the nuclear and microsomal fractions from rat liver nodules and normal liver (1988)
    Springer
    Archives of toxicology 62 (1988), S. 336-340 
    Details
    ISSN: 1432-0738
    Keywords: Drug metabolizing enzymes ; Liver nodules ; Nucleus ; Microsomes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The activities of UDP-glucuronyl transferase, DT-diaphorase, epoxide hydrolase, aryl hydrocarbon hydroxylase, γ-glutamyl transferase and NADPH-cytochrome c reductase were measured in the nuclear and microsomal fractions from normal rat liver and rat liver nodules. Nodules were produced by intermittent feeding of Wistar rats with a standard diet supplemented with 0.05% (w/w) 2-acetylaminofluorene. The nuclear and microsomal fractions were isolated by differential centrifugation. The activities of UDP-glucuronyl transferase, DT-diaphorase, epoxide hydrolase and γ-glutamyl transferase were significantly increased in the nuclear and microsomal fractions obtained from nodules as compared with normal liver. Aryl hydrocarbon hydroxylase activity was decreased in the microsomal fraction from the pathological tissue but not in the nuclear fraction. NADPH-cytochrome c reductase activity was similar in nodular and normal liver tissue. The nuclear/microsomal ratio for phase I reactions in xenobiotic metabolism was increased over normal more than two fold. Thus the nuclear and microsomal systems for drug metabolism are both changed in liver nodules. The relative enhancement of nuclear activating reactions is remarkable in the light of the increased risk for malignant transformation exhibited by nodular cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00293619
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  • 7
    Electronic Resource
    Electronic Resource
    Distribution of 2-naphthol sulphotransferase and its endogenous substrate adenosine 3′-phosphate 5′-phosphosulphate in human tissues (1989)
    Springer
    European journal of clinical pharmacology 37 (1989), S. 317-320 
    Details
    ISSN: 1432-1041
    Keywords: 2-naphthol sulphotransferase ; adenosine 3′-phosphate 5′-phosphosulfate ; liver ; kidney ; lung ; intestine ; tissue distribution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary The activity of sulphotransferase towards 2-naphthol and the concentration of its endogenous substrate, adenosine 3′-phosphate 5′-phosphosulphate (PAPS), have been measured in five specimens of human liver, lung, and kidney, and the mucosa from the ileum and the ascending, descending and sigmoid colon. The activity of 2-naphthol sulphotransferase (mean nmol·min−1·mg−1 protein) was 1.82 (liver); 0.034 (kidney); 0.19 (lung); 0.64 (ileum); 0.47 (ascending colon); 0.50 (descending colon); 0.40 (sigmoid colon). The concentration of PAPS (mean nmol·g−1 wet tissue) was 22.6 (liver); 4.8 (kidney); 4.3 (lung); 12.8 (ileum); 8.1 (ascending colon); 7.5 (descending colon); 6.2 (sigmoid colon). The concentration of PAPS and the activity of 2-naphthol sulphotransferase were higher in the liver than in the extrahepatic tissues. There was significant difference between ileum and ascending colon, both the activity of sulphotransferase and the concentration of PAPS being higher in the former. 2-Naphthol sulphotransferase activity and the concentration of PAPS have consistent distribution patterns. Differences between the tissues studied were more marked for sulphotransferase than for its endogenous substrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00679793
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  • 8
    Electronic Resource
    Electronic Resource
    Plasma protein binding of alpidem in healthy volunteers, in neonates and in liver or renal insufficiency (1989)
    Springer
    European journal of clinical pharmacology 37 (1989), S. 29-32 
    Details
    ISSN: 1432-1041
    Keywords: alpidem ; cirrhotics ; anxiolytics ; placental serum ; renal failure ; plasma protein binding ; neonates
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary The binding of alpidem, a new anxiolytic drug, has been studied in plasma from 6 healthy subjects, 12 patients with renal failure, 12 patients with liver cirrhosis and 12 chronic uraemics maintained on haemodialysis, as well as in 12 serum samples from the placental cord, to represent the situation in the newborn. The unbound fraction was 0.61% (healthy volunteers), 1.31% (newborns), 0.86% (cirrhotic patients), 0.72 (patients with renal failure), 0.70% (before haemodialysis) and 0.79% (after haemodialysis). Binding in the volunteers was significantly different from that in neonates and cirrhotics only. Alpidem became bound to isolated albumin (45 g·l−1) and alpha1-acid glycoprotein (0.75 g·l−1) to 97.2% and 97.1%, respectively. The bound fraction of the drug in a mixture of two proteins was 99.1%. For alpidem, it appears that alpha1-acid glycoprotein may balance the effect of any decrease in the albumin concentration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00609419
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