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  • 1
    Electronic Resource
    Electronic Resource
    Reductive Addition at the W3S44+ Core by Sn2+ or an Unusual Supramolecular System: A Synergetic Reaction Leading to the Host Guest Compound (Me2NH2)6[(SCN)9W3S4SnCl3].cntdot.0.5H2O (1994)
    s.l. : American Chemical Society
    Inorganic chemistry 33 (1994), S. 2243-2247 
    Details
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ic00088a029
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  • 2
    Electronic Resource
    Electronic Resource
    Association to HeLa cells and surface behavior of exogenous gangliosides studied with a fluorescent derivative of GM1 (1990)
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 697-701 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00455a015
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  • 3
    Electronic Resource
    Electronic Resource
    Les gisements d'émeraude de la Cordillère Orientale de la Colombie: Nouvelles données métallogéniques (1990)
    Springer
    Mineralium deposita 25 (1990), S. 105-111 
    Details
    ISSN: 1432-1866
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences
    Notes: Abstract Emerald deposits of Colombia are confined to lower Cretaceous shales of the Eastern Cordillera. The tectonic pattern of the deposits is related to deep reverse and large regional fault systems. Hydrofracturing is the main factor controlling emerald mineralization. It permitted to the hydrothermal solutions to permeate through fractures but also along stratification planes forming in this case stratabound mineralizations. Emerald occurs in calcite veins, veinlets, pockets and brecciated zones associated mainly with pyrite, quartz, parisite, codazzite and fluorite. Emerald mineralization belongs to an epigenetic hydrothermal process. The alternance of arenite-shale formations in the Cretaceous probably played an important role in the accumulation of solutions and in the propagation of the hydrothermal channels. The origin of emerald involves chemical elements mobilized by the fluids in the Cr-V-Fe-Al-Si-bearing black shales. The source of beryllium remains a problem and is discussed in the paper.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00208852
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  • 4
    Electronic Resource
    Electronic Resource
    Minoxidil sulphation in human liver and platelets (1993)
    Springer
    European journal of clinical pharmacology 45 (1993), S. 337-341 
    Details
    ISSN: 1432-1041
    Keywords: Minoxidil ; sulphotransferase ; liver ; extrahepatic tissues ; platelets ; interindividual variability ; adults ; neonates
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary Minoxidil requires to be sulphated to exert its hypotensive effect. We report on interindividual variability in the rate of minoxidil sulphation in 118 specimens of human liver and in platelets obtained from 100 healthy subjects and 100 newborns. The frequency distribution histogram of the hepatic activity of minoxidil sulphotransferase was positively skewed; the mean was 631 pmol · min−1 · mg−1. After logarithmic transformation of the enzyme activity, the frequency distribution histogram became symmetrical and did not significantly deviate from normality. The rate of minoxidil sulphation was not different in platelets from adults (0.74 pmol · min−1 · mg−1) and newborns (1.16 pmol · min−1 · mg−1). The frequency distribution histograms were positively skewed and the results of normal equivalent deviation analysis was compatible with the presence of at least two subgroups of sulphotransferase in liver and platelets. Thus, two phenotypes of sulphotransferase exist in human liver and platelets, and the “extensive sulphator” phenotype contributes to skewing the frequency distribution. In platelets, the percentage of subjects that fall in the two subgroups is different at birth and in adulthood. This can explain the different shape of the frequency distribution in newborn and adult platelets and suggests that platelet minoxidil sulphotransferase undergoes modification after birth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00265951
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  • 5
    Electronic Resource
    Electronic Resource
    Stereoselective inhibition by chloroquine of histamine N-methyltransferase in the human liver and brain (1994)
    Springer
    European journal of clinical pharmacology 47 (1994), S. 345-349 
    Details
    ISSN: 1432-1041
    Keywords: Chloroquine ; Stereoselectivity ; Histamine ; methyltransferase ; liver ; brain ; man
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Abstract This study was designed to determine whether both enantiomers of chloroquine inhibit histamine N-methyltransferase. The mean estimates of IC50 for the d- and l-enantiomers of chloroquine were 4.9 and 17.8 μM (liver), respectively and 6.9 and 21.6 μM (brain), respectively. Ki estimates were significantly lower with d- than with l-chloroquine; hence, d-chloroquine interacts with the enzyme more effectively than l-chloroquine. If the adverse effects of chloroquine are due to the inhibition of histamine N-methyltransferase, therapy with the l-enantiomer might have lower toxicity. The residual activity of histamine N-methyltransferase should reflect both the degree of inhibition by chloroquine and the level of enzyme expression. The rate of histamine methylation was measured in 100 human liver samples and its range and fold of variation were 29% and threefold, respectively. Susceptibility to chloroquine should be greater in subjects with limited expression of histamine N-methyltransferase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00191166
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  • 6
    Electronic Resource
    Electronic Resource
    Sulphation and glucuronidation of ritodrine in human foetal and adult tissues (1993)
    Springer
    European journal of clinical pharmacology 44 (1993), S. 259-264 
    Details
    ISSN: 1432-1041
    Keywords: Ritodrine ; sulphation ; glucuronidation ; man ; adult tissues ; fetal tissues
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary Ritodrine is a β2-adrenoceptor agonist used for the management of preterm labour. It is inactivated by conjugation with sulphate and glucuronic acid. There is more ritodrine sulphate than ritodrine glucuronide in urine from the newborn whereas equal amounts of ritodrine glucoronide and sulphate are excreted in maternal urine [Clin. Pharmacol. Ther 44, 634–641, 1988]. We show that, in the mid-gestational human fetal liver, ritodrine sulphotransferase is well expressed, whereas the glucuronidation of ritodrine is little developed compared to the adult liver. The average sulphotransferase activity was 308 pmol·min−1 per mg protein in fetal (N=48) and 145 pmol·min−1 per mg protein in adult (N=32) liver. The rates of ritodrine sulphation in fetal gut, lung and kidney were higher than in the corresponding adult tissues. The development and tissue distribution patterns of ritodrine sulphotransferase are consistent with those of dopamine sulphotransferase. Ritodrine and dopamine are sulphated by thermolabile enzymes. The activity of glucuronyl transferase was measurable in only 5 of the 48 foetal livers assayed, and in those in which could be assayed, the average activity was 44.6 pmol·min−1 per mg protein, one-tenth of that in adult livers (524 pmol·min−1 per mg protein).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00271368
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  • 7
    Electronic Resource
    Electronic Resource
    Human liver budesonide sulphotransferase is inhibited by testosterone and correlates with by testosterone sulphotransferase (1994)
    Springer
    European journal of clinical pharmacology 46 (1994), S. 49-54 
    Details
    ISSN: 1432-1041
    Keywords: Budesonide ; liver ; man ; sulphotransferase ; testosterone ; drug metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Abstract Budesonide, a corticosteroid used in the treatment of asthma and allergic reactions, is almost entirely cleared by metabolism in man. We describe the sulphation of budesonide in human liver and lung and provide evidences that the sulphation of budesonide is catalysed by testosterone sulphotransferase. A rapid and reproducible radiometric assay for budesonide sulphotransferase is described. Liver specimens were obtained from 35 men and 65 women and lung specimens from 2 women and 17 men. The average hepatic budesonide sulphation rate was significantly higher in men (41.1 pmol·min−1·ml−1) than women (28.2 pmol·min−1·mg−1). In the lung, the mean budesonide sulphation rate was 5.0 pmol·min−1·mg−1. Testosterone strongly inhibited the hepatic sulphation of budesonide, whereas p-nitrophenol and dopamine were poor inhibitors; the IC50 was 7.0 uM (testosterone), 320 uM (p-nitrophenol) and 510 uM (dopamine). The hepatic rates of testosterone, p-nitrophenol and dopamine sulphation were measured in the same samples assayed for budesonide sulphotransferase. There was a correlation between the hepatic rates of budesonide and testosterone sulphation (P〈0.001; r=0.810). The activity of testosterone sulphotransferase was significantly greater in men than women (22.0 vs. 17.2 pmol·min−1·mg−1), wheres those of dopamine and p-nitrophenol sulphotransferase were not sex dependent. The hepatic activity of budesonide sulphotransferase parallels that of testosterone suggesting that sulphation is an important reaction in the metabolism of budesonide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00195915
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  • 8
    Electronic Resource
    Electronic Resource
    Distribution of UDP-glucuronosyltransferase and its endogenous substrate uridine 5′-diphosphoglucuronic acid in human tissues (1991)
    Springer
    European journal of clinical pharmacology 41 (1991), S. 345-350 
    Details
    ISSN: 1432-1041
    Keywords: UDP-glucuronosyltransferase ; Drug glucuronidation ; 5′-uridine diphosphoglucuronic acid ; human tissues ; enzyme kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary The activity of UDP-glucuronosyltransferase (UDPGT) and the concentration of its endogenous substrate, 5′-diphosphoglucuronic acid (UDPGA), have been measured in human liver, kidney, lung and intestinal mucosa. The activity of UDPGT was tissue- and substrate-dependent. The liver/kidney and liver/intestine ratios for UDPGT varied over one order of magnitude with three substrates. The highest activity of UDGPT in extrahepatic tissues was in the kidney, with 1-naphthol as substrate; it was about half of the hepatic activity. The concentration (μmol · kg−1) of UDPGA was 279 (liver), 17.4 (kidney), 19.3 (intestinal mucosa) and 17.2 (lung), it was at least 15-fold higher in liver than the other tissues, and the concentration in kidney, lung and intestinal mucosa was similar. The kinetics of UDPGT in a liver homogenate at varying concentrations of UDPGA and fixed concentration of 1-naphthol, ethinyloestradiol, and morphine was also measured. The apparent kM for UDPGT depended upon the chemical nature of the UDPGA-acceptor substrate; average values of kM were 63, 300, and 700 μmol · 1−1 for 1-naphthol, ethinyloestradiol and morphine respectively. These values are, respectively, lower, similar to and higher than the hepatic concentration of UDPGA. Under certain circumstances UDPGA may be the limiting factor in the in vivo glucuronidation of drugs by extrahepatic tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00314965
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  • 9
    Electronic Resource
    Electronic Resource
    (+) and (−) terbutaline are sulphated at a higher rate in human intestine than in liver (1993)
    Springer
    European journal of clinical pharmacology 45 (1993), S. 483-487 
    Details
    ISSN: 1432-1041
    Keywords: Terbutaline ; Drug metabolism ; sulphotransferases ; liver ; intestine ; lung ; man ; stereoselective conjugation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary The sulphation of (+) and (−) terbutaline was investigated in specimens of human intestinal mucosa isolated from the duodenum, ileum, ascending colon and sigmoid colon and in specimens of liver and lung. The lung specimens came from 8 current smokers and 11 ex-smokers, the latter having stopped at least 3 months before surgery. The rates (pmol·min−1·mg protein−1) of (+) and (−) terbutaline sulphation were 1195 and 948 (duodenum), 415 and 317 (ileum), 268 and 166 (ascending colon), 263 and 193 (sigmoid colon) and 45 and 34 (liver), respectively. Terbutaline sulphotransferase was more active in the small and large intestine than in the liver. In the lung, the rate of (+) terbutaline sulphation was 118 (ex-smokers) and 82 (smokers), and for (−) terbutaline it was 82 (ex-smokers) and 56 (smokers). In the gut, the activity of catechol sulphotransferase was significantly correlated with that of (+)- and (−)- terbutaline sulphotransferase whereas no correlation was found with phenol sulphotransferase. This correlation, the finding of the higher activity of terbutaline sulphotransferase in gut than in liver, and the pronounced thermal inactivation of the enzyme, are all consistent with the view that catechol sulphotransferase has a role in the sulphation of terbutaline.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00315522
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  • 10
    Electronic Resource
    Electronic Resource
    NK-2 Receptor Agonists and Antagonists (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 632 (1991), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1991.tb33106.x
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