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  • 1
    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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  • 2
    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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  • 3
    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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  • 4
    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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  • 5
    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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