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  • 11
    Electronic Resource
    Electronic Resource
    Effect of phenylbutazone on the binding of vitamin K antagonists to albumin (1973)
    Springer
    European journal of clinical pharmacology 6 (1973), S. 15-18 
    Details
    ISSN: 1432-1041
    Keywords: Warfarin ; ethyl biscoumacetate ; acenocoumarin ; phenindione ; fluoropindione ; albumin binding ; phenylbutazone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary Ethyl biscoumacetate and acenocoumarin are bound to the same sites on human albumin as warfarin. Phenindione and fluorophenindione are bound to other sites. Phenylbutazone inhibits binding of the former but has no effect on the latter. These results can account for the fact that clinical reports of interaction between phenylbutazone and vitamin K antagonists involve only coumarin drugs, especially warfarin, and not phenindione derivates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00561795
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  • 12
    Electronic Resource
    Electronic Resource
    Effect of sodium chlorophenoxyisobutyrate on the binding of vitamin K antagonists to human albumin in vitro (1974)
    Springer
    Cellular and molecular life sciences 30 (1974), S. 460-461 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Résumé In vitro, le chlorophénoxyisobutyrate de sodium (CPIB) s'oppose à la fixation sur l'albumine humaine des dérivés de la coumarine mais ne modifie pas celle des phénindiones. Les races accidents hémorragiques observés lors de l'emploi simultané de CPIB et d'un dérivé de la phénindione ne peuvent s'expliquer par une défixation, due au CPIB, de l'anticoagulant fixé sur l'albumine plamatique.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01926292
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  • 13
    Electronic Resource
    Electronic Resource
    Die Bindung von Erythromycin an Serumproteine des Menschen bei verschiedenen Infektionen (1982)
    Springer
    Infection 10 (1982), S. S113 
    Details
    ISSN: 1439-0973
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary A large amount of the erythromycin in the serum is bound to acidic α1-glycoprotein; the exact share is dependent on the concentration. The concentration of acidic α1-glycoprotein can be elevated during infections. Thus, a larger amount of the erythromycin is bound, leaving less free antibiotic.
    Notes: Zusammenfassung Saures α1-Glycoprotein bindet konzentrationsabhängig den größten Anteil des Erythromycins im Serum. Die Konzentration des sauren α1-Glycoproteins kann bei Infektionen erhöht sein; damit nimmt die Bindung des Erythromycins zu und der freie Antibiotika-Anteil ab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01640868
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  • 14
    Electronic Resource
    Electronic Resource
    Study of deuterium isotope effects on protein binding by gas chromatography/mass spectrometry. Caffeine and deuterated isotopomers (1987)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 14 (1987), S. 653-657 
    Details
    ISSN: 0887-6134
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A study of the binding to human serum albumin (HSA) of caffeine and its deuterated isotopomers, 1-C2H3-, 3-C2H3-, 1,7-(C2H3)2-, 3,7-(C2H3)2- and 1,3,7-(C2H3)3-caffeine, was performed by equilibrium dialysis. Free and bound fractions were measured by gas chromatography/mass spectrometry. Important and significant (Fischer and Student tests) isotope effects were observed on binding parameters: sites total concentration (N = 1732) μM for 1,3,7-(C2H3)3-caffeine versus 822 μM for caffeine; number of sites (n = 3 for 1,3,7-(C2H3)3-caffeine v. 1 for caffeine); and extent of binding (46% for 1,3,7-(C2H3)3-caffeine v. 27% for caffeine).A study of competition for HSA binding between caffeine and its 1,3,7-(C2H3)3- and 3,7-(C2H3)2-isotopomers confirmed the results obtained in direct binding studies. These isotope effects are discussed in terms of (a) tools for molecular pharmacology, (b) precautions to be taken when such labelled drugs are used in clinical pharmacology.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200141115
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  • 15
    Electronic Resource
    Electronic Resource
    Study of isotope effects on protein binding by gas chromatography/mass spectrometry of theophylline-phenobarbitone and 2H, 13C, 15N isotopomers (1988)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 17 (1988), S. 245-250 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: We describe a comparative study of human serum albumin (HSA) binding by equilibrium dialysis (pH 7.4, 37°C, 3 h) for two groups of isotopic analogues: theophylline and 1-C(2H3)theophylline; unlabelled, 5(ethyl(2H5)),-5(phenyl(2H5)) and 1,3-15N;2-13C-phenobarbitone. Bound and free drug fractions are quantified by combined gas chromatography/mass spectrometry. In three instances, protein binding parameters are greatly affected by isotopic substitution, namely for: theophylline and 1-C(2H3)theophylline with isotope effects on total binding site concentration (N), affinity constant (Ka) and extent of HSA binding (%) respectively, equal to: NL/NH=0.51; KaL/KaH = 1.78; %L/%H = 0.96 (L (light) and H (heavy) represent the unlabelled and labelled analogue respectively); phenobarbitone/-5-(phenyl(2H5))phenobarbitone, NL/NH = 1.72; KaL/KaH = 0/56; %L/%H = 1.26; phenobarbitone/1,3-15N;2-13C phenobarbitone, NL/NH = 2.95; KaL/KaH = 0.44; %L/%H = 1.32, together with a change from one (saturable) to two (saturable + non-saturable) families of albumin binding sites in the latter case. Contrasting with these data, no HSA binding isotope effect was observed on phenobarbitone C5 ethyl deuteration.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200170403
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