Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites (1989)
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 8639-8645 
    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/bi00447a054
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    INTERACTION OF SOME DRUGS, METAL IONS, AND ALCOHOLS WITH RAT LIVER MICROSOMES AS STUDIED WITH A FLUORESCENT PROBE (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 1 (1974), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: SUMMARY 1. The effects of various compounds on the fluorescence of microsome-bound 1-anilino-8-naphthalene sulphonate (ANS) have been studied.2. Cationic drugs and divalent metal cations enhance the fluorescence of microsome-bound ANS whereas anionic drugs and primary aliphatic alcohols decrease it.3. No changes were observed in the fluorescence lifetime or emission maximum of ANS and it was concluded that there were no significant changes in the quantum yield of ANS fluorescence.4. The changes in fluorescence are shown to be related to changes in ANS binding.5. The results suggest that drug-induced changes in the binding of ANS to the microsomal membrane reflect a change in the net charge on the membrane as a result of the binding of a charged drug and that changes in ANS fluorescence cannot be directly interpreted as changes in the structure of the membrane.6. Primary aliphatic alcohols displace ANS from the microsomal membrane but cause no change in quantum yield. It is suggested that the alcohols change the net charge on the membrane either by exposure of negative charges or occlusion of positive charges.7. The changes in ANS fluorescence can be used as a measure of the interaction of various drugs with the microsomal membrane. Apparent binding constants determined by this method for various drugs fall in the concentration ranges over which the drugs are reported to induce changes in membrane function in various in vitro systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1974.tb00563.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    A SIMPLE HPLC ASSAY FOR URINARY PARACETAMOL METABOLITES AND ITS USE TO CHARACTERIZE THE C3H MOUSE AS A MODEL FOR PARACETAMOL METABOLISM STUDIES (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 11 (1984), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. A high performance liquid chromatographic (HPLC) assay for unchanged paracetamol and its glucuronide, sulphate, cysteine and mercapturic acid conjugates in the urine of man, mouse and rat is described. The method is simple, rapid and reproducible.2. The metabolite assay has been used to characterize the male C3H mouse, which shows sensitivity to paracetamol toxicity similar to man, as a model for paracetamol metabolism studies.3. In male C3H mice there was no evidence to suggest saturability of the glucuronidation pathway on increasing the paracetamol dose from 50 to 300 mg/kg. By contrast, the metabolic ratio and fractional excretion of both the sulphate and glutathione-derived conjugates decreased with increasing paracetamol dose.4. For animals administered a 200 mg/kg dose of paracetamol, pretreatment with phenobarbitone or 3-methylcholanthrene increased the fractional excretion and metabolic ratio of the glutathione-derived and glucuronic acid conjugates. Piperonyl butoxide pretreatment of animals administered the same dose of paracetamol inhibited glutathione and glucuronic acid conjugation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1984.tb00258.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Spectroscopic techniques in the study of protein binding. A fluorescence technique for the evaluation of the albumin binding and displacement of warfarin and warfarin-alcohol (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 2 (1975), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. The binding of racemic mixtures of warfarin and warfarin-alcohol to human serum albumin (HSA) is accompanied by an increase in the fluorescence quantum yield of these compounds. This property has been used to measure the characteristics of the binding of warfarin and warfarin-alcohol to HSA at 22°C and 37°C. Within the limits of the technique, no significant differences between the number of binding sites and strength of binding at the tight site at either temperature were observed.2. The fluorescence of warfarin and warfarin-alcohol was used to label their binding site on HSA and to study the effects of other drugs on their binding. The results indicate that these two molecules are bound to the same site on HSA.3. The validity of using changes in the fluorescence of warfarin as a measure of its displacement from HSA was investigated. Good correlations were observed between drug-induced decreases in the fluorescence of bound warfarin and displacement as measured by equilibrium dialysis. The displacement of warfarin, as detected by fluorescence, correlates well with the increase in free warfarin resulting from addition of therapeutic drug concentrations to undiluted human serum.4. The most potent displacing agents, by all the methods used, were iophenoxic acid, phenylbutazone and oxyphenylbutazone. The first of these is no longer used clinically, but the latter two are and have been reported to cause hypoprothromin-aemia by displacing warfarin from HSA. The present study indicates that changes in the fluorescence of warfarin bound to HSA can be used to measure displacement of bound warfarin and to screen drugs that may cause clinically significant interactions by this mechanism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1975.tb01826.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    IMMUNOCHEMICAL AND CATALYTICAL CHARACTERIZATION OF THE HUMAN LIVER NADPH-CYTOCHROME P450 REDUCTASE (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 16 (1989), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. The NADPH-cytochrome P450 reductases (EC 1.6.2.4) from human and rabbit liver have been purified to electrophoretic homogeneity. The human reductase had an apparent monomeric molecular weight of 77 500 and the rabbit enzyme of 76 500.2. Both flavoproteins exhibited typical flavoprotein spectra and contained equimolar quantities of FAD and FMN. The two reductases were catalytically active in reducing cytochrome c, ferricyanide and dichlorophenolindophenol, and in supporting rabbit liver cytochrome P450 Form 4 metabolism of 2-acetylamino-fluorene.3. An antibody raised in the goat against the human enzyme formed a precipitin line with the human reductase in a double-diffusion assay, but did not react with the rabbit reductase. Similarly, an antibody raised in the goat against the rabbit reductase formed a precipitin line with the rabbit enzyme, but did not cross-react with the human reductase.4. Both antibodies inhibited cytochrome c reduction by the two reductases suggesting some immunochemical recognition.5. Immunochemical cross-reactivity was confirmed when both reductases were subjected to the more sensitive immunoblot technique using either anti-human or anti-rabbit reductase IgG.6. The human and rabbit reductases are essentially similar in amino acid composition, except that the former has larger amounts of serine and glycine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1989.tb01536.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Biochemical validation of self-reported caffeine consumption during caffeine fading (1988)
    Springer
    Journal of behavioral medicine 11 (1988), S. 15-30 
    Details
    ISSN: 1573-3521
    Keywords: caffeine ; biochemical validation ; fading
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Psychology
    Notes: Abstract Increasing concern about caffeine as a drug with potential for abuse has resulted in the development of procedures for effecting reductions in caffeine consumption among heavy users. However, the reliability of reported findings may be questioned, since previous studies have relied on subject self-report as the principal measure of caffeine use. The present study employed bioanalytic methods for assessing the reliability of self-reported caffeine intake during a caffeine-fading regime. Twelve subjects, each with a history of heavy caffeine use, provided baseline, treatment, and follow-up blood samples which were assayed for caffeine and its major metabolites. General support was provided for the reliability of self-report as a measure of caffeine consumption. The general efficacy of caffeine fading was also supported, although there were indications that maintenance effects may have been over-estimated in previous studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00846166
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...