Relevant bibliographies by topics / Human liver microsomes

Academic literature on the topic 'Human liver microsomes'

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Published: 4 June 2021
Last updated: 25 January 2023

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Journal articles on the topic "Human liver microsomes"

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Minoda, Yuko, and Evan D. Kharasch. "Halothane-dependent Lipid Peroxidation in Human Liver Microsomes Is Catalyzed by Cytochrome P4502A6 (CYP2A6)." Anesthesiology 95, no. 2 (August 1, 2001): 509–14. http://dx.doi.org/10.1097/00000542-200108000-00037.

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Background Halothane is extensively (approximately 50%) metabolized in humans and undergoes both oxidative and reductive cytochrome P450-catalyzed hepatic biotransformation. Halothane is reduced under low oxygen tensions by CYP2A6 and CYP3A4 in human liver microsome to an unstable free radical, and then to the volatile metabolites chlorodifluoroethene (CDE) and chlorotrifluoroethane (CTE). The free radical is also thought to initiate lipid peroxidation. Halothane-dependent lipid peroxidation has been shown in animals in vitro and in vivo but has not been evaluated in humans. This investigation tested the hypothesis that halothane causes lipid peroxidation in human liver microsomes, identified P450 isoforms responsible for halothane-dependent lipid peroxidation, and tested the hypothesis that lipid peroxidation is prevented by inhibiting halothane reduction. Methods Halothane metabolism was determined using human liver microsomes or cDNA-expressed P450. Lipid peroxidation was quantified by malondialdehyde (MDA) formation using high-pressure liquid chromatography-ultraviolet analysis of the thiobarbituric acid-MDA adduct. CTE and CDE were determined by gas chromatography-mass spectrometry. Results Halothane caused MDA formation in human liver microsomes at rates much lower than in rat liver microsomes. Human liver microsomal MDA production exhibited biphasic enzyme kinetics, similar to CDE and CTE production. MDA production was inhibited by the CYP2A6 inhibitor methoxsalen but not by the CYP3A4 inhibitor troleandomycin. Halothane-dependent MDA production was catalyzed by cDNA-expressed CYP2A6 but not CYP3A4 or P450 reductase alone. CYP2A6-catalyzed MDA production was inhibited by methoxsalen or anti-CYP2A6 antibody. Conclusions Halothane causes lipid peroxidation in human liver microsomes, which is catalyzed by CYP2A6, and inhibition of halothane reduction prevents halothane-dependent lipid peroxidation in vitro.
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Myllynen, P., P. Pienimäki, H. Raunio, and K. Vähäkangas. "Microsomal metabolism of carbamazepine and oxcarbazepine in liver and placenta." Human & Experimental Toxicology 17, no. 12 (December 1998): 668–76. http://dx.doi.org/10.1177/096032719801701204.

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Metabolism of both carbamazepine (CBZ) and oxcarbaze-pine (OCBZ) were catalyzed by human liver microsomes and microsomes from livers of CBZ-induced or non-induced C57BL/6 mice. Human placental microsomes metabolized only OCBZ. Mouse liver microsomes metabolized CBZ to carbamazepine-10,11-epoxide (CBZ-E), 10- hydroxy-10,11-dihydro-carbamazepine (10-OH-CBZ), 3- hydroxy-carbamazepine (3-OH-CBZ), 10,11-trans-dihydroxy-10,11-dihydro-carbamazepine (10,11-D) and to an unidentified metabolite. CBZ-pretreatment of mice increased both ethoxyresorufin O-deethylase activity in the liver and the amount of CBZ-E in microsomal incubations regardless of the age of mice. Human liver microsomes catalyzed the formation of CBZ to 9-hydroxymethyl-10-carbamoyl acridan (9-AC) in addition to CBZ-E, 3-OH-CBZ and 10-OH-CBZ. OCBZ was metabolized to its active metabolite in all incubations. An unknown metabolite was also present in some of the incubations. Human liver microsomes catalyzed only minute covalent binding of CBZ and OCBZ to DNA. Binding of OCBZ was, however, one order of magnitude greater than binding of CBZ. Human placental micro-somes from the mothers on CBZ therapy did not catalyze CBZ metabolism. The same microsomes catalyzed OCBZ metabolism to 10-OH-CBZ and to an unknown metabolite. These results indicate autoinduction in CBZ metabolism in mouse liver. Due to the higher binding of OCBZ than CBZ to DNA in vitro, further studies on the potential mutagenicity of OCBZ may be warranted.
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Barnes, T. S., M. D. Burke, and W. T. Melvin. "Differences in adult and foetal human cytochrome P-450 forms recognized by monoclonal antibodies with specificity for the P450III family." Biochemical Journal 260, no. 3 (June 15, 1989): 635–40. http://dx.doi.org/10.1042/bj2600635.

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Six murine monoclonal antibodies raised against a major human adult liver cytochrome P-450 (P-450) of the PCN family (P450III) detected a protein in human foetal liver microsomes (microsomal fractions) which had an approx. 1 kDa higher molecular mass on SDS/polyacrylamide-gel electrophoresis than the protein recognized in human adult liver microsomes. Although each of the antibodies recognized both the adult and the foetal forms, antibody HL4 showed higher affinity for the foetal form. Recognition by the monoclonal antibodies of peptides generated by proteolytic cleavage of microsomal proteins showed different patterns for the adult and foetal forms. It is concluded that the foetal P-450 form recognized by antibodies to the major human adult liver form P450hA7, although structurally similar, is either a distinct P-450 isoenzyme or that the adult and foetal proteins have different covalent modification. Immunoquantification experiments showed comparable levels of the P-450 forms in adult and foetal liver, although there appeared to be less inter-individual variation in foetal livers.
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George, R., P. J. Davis, L. Luong, and M. J. Poznansky. "Cholesterol-mediated regulation of HMG-CoA reductase in microsomes from human skin fibroblasts and rat liver." Biochemistry and Cell Biology 68, no. 3 (March 1, 1990): 674–79. http://dx.doi.org/10.1139/o90-097.

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3-Hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase activity was determined in microsomes from human skin fibroblasts and rat liver that had been variously manipulated in vivo or in tissue culture to up- and down-regulate the enzyme. The cholesterol content of these microsomal preparations was then altered by depletion to or enrichment from either cholesterol-free or cholesterol-rich lipid vesicles. Microsomes from human skin fibroblasts responded to cholesterol depletion by increasing HMG-CoA reductase activity and by decreasing it in response to cholesterol enrichment. This was independent of the initial enzyme activity or the tissue culture conditions. Alterations in cholesterol content of rat liver microsomes in vitro failed to demonstrate any significant changes in HMG-CoA reductase activity whether the microsomes started with low enzyme activity (cholesterol-fed rats) or with high enzyme activity (cholestyramine-treated rats). The results are discussed in relation to previously published data and in respect to differences in the control of the human skin fibroblast and rat liver enzymes.Key words: cholesterol, HMG-CoA reductase, microsomes, fibroblasts, rat liver.
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Nguyen, Ngoc, Ngoc Cao, Thi Nguyen, Thien-Kim Le, Gun Cha, Soo-Keun Choi, Jae-Gu Pan, Soo-Jin Yeom, Hyung-Sik Kang, and Chul-Ho Yun. "Regioselective Hydroxylation of Phloretin, a Bioactive Compound from Apples, by Human Cytochrome P450 Enzymes." Pharmaceuticals 13, no. 11 (October 22, 2020): 330. http://dx.doi.org/10.3390/ph13110330.

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Phloretin, the major polyphenol compound in apples and apple products, is interesting because it shows beneficial effects on human health. It is mainly found as a form of glucoside, phlorizin. However, the metabolic pathway of phloretin in humans has not been reported. Therefore, identifying phloretin metabolites made in human liver microsomes and the human cytochrome P450 (P450) enzymes to make them is interesting. In this study, the roles of human liver P450s for phloretin oxidation were examined using human liver microsomes and recombinant human liver P450s. One major metabolite of phloretin in human liver microsomes was 3-OH phloretin, which is the same product of a bacterial CYP102A1-catalyzed reaction of phloretin. CYP3A4 and CYP2C19 showed kcat values of 3.1 and 5.8 min−1, respectively. However, CYP3A4 has a 3.3-fold lower Km value than CYP2C19. The catalytic efficiency of a CYP3A4-catalyzed reaction is 1.8-fold higher than a reaction catalyzed by CYP2C19. Whole-cell biotransformation with CYP3A4 was achieved 0.16 mM h−1 productivity for 3-OH phlorein from 8 mM phloretin at optimal condition. Phloretin was a potent inhibitor of CYP3A4-catalyzed testosterone 6β-hydroxylation activity. Antibodies against CYP3A4 inhibited up to 90% of the microsomal activity of phloretin 3-hydroxylation. The immunoinhibition effect of anti-2C19 is much lower than that of anti-CYP3A4. Thus, CYP3A4 majorly contributes to the human liver microsomal phloretin 3-hydroxylation, and CYP2C19 has a minor role.
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Court, Michael H., Su X. Duan, Leah M. Hesse, Karthik Venkatakrishnan, and David J. Greenblatt. "Cytochrome P-450 2B6 Is Responsible for Interindividual Variability of Propofol Hydroxylation by Human Liver Microsomes." Anesthesiology 94, no. 1 (January 1, 2001): 110–19. http://dx.doi.org/10.1097/00000542-200101000-00021.

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Background Oxidation of propofol to 4-hydroxypropofol represents a significant pathway in the metabolism of this anesthetic agent in humans. The aim of this study was to identify the principal cytochrome P-450 (CYP) isoforms mediating this biotransformation. Methods Propofol hydroxylation activities and enzyme kinetics were determined using human liver microsomes and cDNA-expressed CYPs. CYP-specific marker activities and CYP2B6 protein content were also quantified in hepatic microsomes for correlational analyses. Finally, inhibitory antibodies were used to ascertain the relative contribution of CYPs to propofol hydroxylation by hepatic microsomes. Results Propofol hydroxylation by hepatic microsomes showed more than 19-fold variability and was most closely correlated to CYP2B6 protein content (r = 0.904), and the CYP2B6 marker activities, S-mephenytoin N-demethylation (r = 0.919) and bupropion hydroxylation (r = 0.854). High- and intermediate-activity livers demonstrated high-affinity enzyme kinetics (K(m) < 8 microm), whereas low-activity livers displayed low-affinity kinetics (K(m) > 80 microm). All of the CYPs evaluated were capable of hydroxylating propofol; however, CYP2B6 and CYP2C9 were most active. Kinetic analysis indicated that CYP2B6 is a high-affinity (K(m) = 10 +/- 2 microm; mean +/- SE of the estimate), high-capacity enzyme, whereas CYP2C9 is a low-affinity (K(m) = 41 +/- 8 microm), high-capacity enzyme. Furthermore, immunoinhibition showed a greater contribution of CYP2B6 (56 +/- 22% inhibition; mean +/- SD) compared with CYP2C isoforms (16 +/- 7% inhibition) to hepatic microsomal activity. Conclusions Cytochrome P-450 2B6, and to a lesser extent CYP2C9, contribute to the oxidative metabolism of propofol. However, CYP2B6 is the principal determinant of interindividual variability in the hydroxylation of this drug by human liver microsomes.
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Milewich, L., P. C. MacDonald, and B. R. Carr. "Activity of 17β-hydroxysteroid oxidoreductase in tissues of the human fetus." Journal of Endocrinology 123, no. 3 (December 1989): 509–18. http://dx.doi.org/10.1677/joe.0.1230509.

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ABSTRACT The interconversion of oestrone and oestradiol, androstenedione and testosterone, and dehydroepi-androsterone and 5-androstene-3β,17β-diol in mammalian tissues is catalysed by 17β-hydroxysteroid oxidoreductase (17β-HSOR). To identify tissue sites of 17β-HSOR activity in the human fetus, microsomal fractions from 15 different fetal tissues obtained from first and second trimester pregnancies were used for evaluation of enzymatic activity by use of [17α-3H] oestradiol as the substrate and NADP+ as the co-factor. With these reagents, the enzyme-catalysed reaction led to the production of both non-radiolabelled oestrone and NADP3H in equimolar amounts; the radioactivity associated with NADP3H was used to quantify 17β-HSOR activity. Activity of 17β-HSOR was present in microsomes of all the tissues evaluated. The specific activity of the enzyme was highest in liver and placental microsomes. The interconversion of oestradiol and oestrone in microsomal fractions of nine different fetal tissues was studied by the use of substrates labelled with tritium at stable nuclear positions ([6,7-3H]oestradiol and [6,7-3H]oestrone). The products, [3H]oestrone and [3H]oestradiol, were quantified by the use of established techniques; other metabolites formed in these incubations were not identified. The reductive pathway of metabolism (oestrone to oestradiol) appeared to be favoured in microsomal fractions prepared from placenta, fetal zone of the adrenal gland and, possibly, lung. The oxidative pathway (oestradiol to oestrone) appeared to be favoured in microsomes prepared from liver, intestine, stomach, kidney, brain and heart. 17β-HSOR activity in fetal liver also was assessed by the use of fresh and frozen-thawed tissue, homogenate, subcellular fractions, and, also, in primary hepatocytes maintained in culture; the specific activity of the enzyme was highest in the microsomal fraction of liver tissue and 17β-HSOR activity in liver microsomes was linear with time of incubation up to 1 h. In hepatocytes, the enzymatic activity was linear with time of incubation up to 2 h and with cell number up to 2·5 × 105 cells/ml; the apparent Michaelis constant of hepatocyte 17β-HSOR for oestradiol was 11 μmol/l. The specific activity of 17β-HSOR did not change after pretreatment of hepatocytes for 24 h with insulin, glucagon or dexamethasone. Journal of Endocrinology (1989) 123, 509–518
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Wang, Li, Zhe Wang, Meng-ming Xia, Ying-ying Wang, Hai-yun Wang, and Guo-xin Hu. "Inhibitory effect of silybin on pharmacokinetics of imatinib in vivo and in vitro." Canadian Journal of Physiology and Pharmacology 92, no. 11 (November 2014): 961–64. http://dx.doi.org/10.1139/cjpp-2014-0260.

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The objective of this work was to investigate the effect of orally administered silybin on the pharmacokinetics of imatinib in rats and the metabolism of imatinib in human liver microsome and rat liver microsomes. Eighteen healthy male SD rats were randomly divided into 3 groups: group A (control group), group B (received multiple doses of 50 mg·kg−1 silybin for 15 consecutive days), and group C (received a single dose of 50 mg·kg−1 silybin). A single dose of imatinib was administered orally 30 min after administration of silybin (50 mg·kg−1). Imatinib plasma levels were measured by UPLC-MS/MS, and pharmacokinetic parameters were calculated by DAS 3.0 software (Bontz Inc., Beijing, China). In addition, human and rat liver microsome were performed to determine the effects of silybin metabolism of imatinib in vitro. The multiple doses or single dose of 50 mg·kg−1 silybin significantly decreased the area under the curve (0-t) of imatinib (p < 0.01). And the half-life (t1/2) of imatinib is significantly increased (p < 0.05 and p < 0.01, respectively). Also, silybin showed inhibitory effect on human and rat microsomes, the IC50 of silybin were 26.42 μmol·L−1 and 49.12 μmol·L−1 in human and rat liver microsomes, respectively. These results indicate that more attention should be paid to when imatinib is administrated combined with silybin.
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Senler, T. I., W. L. Dean, L. F. Murray, and J. L. Wittliff. "Quantification of cytochrome P-450-dependent cyclohexane hydroxylase activity in normal and neoplastic reproductive tissues." Biochemical Journal 227, no. 2 (April 15, 1985): 379–87. http://dx.doi.org/10.1042/bj2270379.

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It is well established that liver microsomal cytochrome P-450 participates in steroid metabolism and probably also in the metabolism of anti-oestrogens such as tamoxifen (Nolvadex). Thus it is possible that variations in cytochrome P-450 levels may influence the responsiveness of human breast and endometrial carcinomas to endocrine therapy. Therefore a simple sensitive spectrophotometric assay for determining levels of cytochrome P-450-dependent cyclohexane hydroxylation activity in breast and uterine microsomes (microsomal fractions) has been developed. Cyclohexane was chosen as a substrate because of the relatively high levels of cyclohexane hydroxylase activity in tumour microsomes and because cyclohexane serves as a substrate for several forms of cytochrome P-450. As previously described [Senler, Dean, Pierce & Wittliff (1985) Anal. Biochem. 144, 152-158], a direct method utilizing isotope-dilution/gas chromatography-mass spectrometry was also developed in order to confirm the results of the spectrophotometric assay. The average activity (cyclohexane-dependent NADPH oxidation) for 139 human breast-tumour microsome preparations was 1.34 nmol/min per mg, which is in the range of that found in untreated mammalian liver (1-3 nmol/min per mg). Also, high enzyme activity was demonstrated in human ovary, normal uterus as well as uterine leiomyomas. Endocrine status appeared to influence enzyme levels, in that mammary tissue from virgin rats contained significantly (P less than 0.025) higher amounts of activity than did tissues from either pregnant or lactating rats. Furthermore, carbon monoxide, as well as an antibody against rat liver cytochrome P-450, completely inhibited NADPH oxidation by breast-carcinoma microsomes. These results strengthen our hypothesis that tumours with high levels of cytochrome P-450 may have a reduced response to additive endocrine therapy.
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Svobodová, Martina, Markéta Martínková, Eva Frei, and Marie Stiborová. "Identification of human enzymes oxidizing a human metabolite of carcinogenic 2-nitroanisole, 2-nitrophenol. Evidence for its oxidative detoxification by human cytochromes P450." Collection of Czechoslovak Chemical Communications 75, no. 6 (2010): 703–19. http://dx.doi.org/10.1135/cccc2010023.

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2-Nitrophenol (2-NP) is the major detoxification metabolite of an important industrial pollutant and a potent carcinogen, 2-nitroanisole (2-NA). Here, we characterized the product of 2-NP metabolism catalyzed by human, rat, rabbit and mouse hepatic microsomes containing cytochromes P450 (CYPs) and identified the major human CYP enzymes participating in this process. The 2-NP metabolite was characterized by mass spectrometry and co-chromatography on HPLC with a synthetic standard, 2,5-dihydroxynitrobenzene (2,5-DNB) to be 2,5-DNB. No nitroreductive metabolism leading to the formation of N-(2-hydroxyphenyl)hydroxylamine or o-aminophenol was evident by all tested hepatic microsomes. Likewise, no DNA binding of 2-NP metabolite(s) measured with the 32P-postlabeling technique was detectable in hepatic microsomes. Therefore, hepatic microsomal CYP enzymes participate in 2-NP metabolism that does not lead to its activation to species binding to DNA. Selective inhibitors of human CYPs were used to characterize CYPs oxidizing 2-NP in human livers. Based on these inhibitory studies, we attribute most of 2-NP oxidation in human liver to CYP2E1, 3A4, 2A6, 2C and 2D6. Among recombinant human CYP enzymes tested in this study, CYP2E1, 2A6 and 2B6 were the most effective enzymes oxidizing 2-NP. Oxidation of 2-NP by human CYP2E1 exhibits the Michaelis-Menten kinetics, having the Km value of 0.21 mM. The results found in this study, the first report on the metabolism of 2-NP by human hepatic microsomes and human CYP enzymes, demonstrate that CYP2E1 is the major enzyme oxidizing this compound in human.
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Dissertations / Theses on the topic "Human liver microsomes"

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Emery, Maurice George. "Aspects of human CYP 2E1 regulation in health and disease /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/7943.

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McLure, James Alexander, and james mclure@flinders edu au. "Physicochemical determinants of the non-specific binding of drugs to human liver microsomes." Flinders University. Medicine, 2008. http://catalogue.flinders.edu.au./local/adt/public/adt-SFU20081102.165952.

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Accurate determination of the in vitro kinetic parameters Km (Michaelis constant) and Ki (inhibition constant) is critical for the quantitative prediction of in vivo drug clearance and the magnitude of inhibitory drug interactions. A cause of inaccuracy in vitro arises from the assumption that all drug added to an incubation mixture is available for metabolism or inhibition. Many drugs bind non-specifically to the membrane of the in vitro enzyme source. The aims of this thesis were to: 1) investigate the comparative importance of lipophilicity (as log P), and pKa as determinants of the non-specific binding of drugs to human liver microsomes; 2) develop and validate an ANS fluorescence technique for measuring the non-specific binding of drugs to human liver microsomes; 3) characterise the non-specific binding of a large dataset of physicochemically diverse drugs using the ANS fluorescence procedure; 4) evaluate relationships between selected physicochemical characteristics and the extent of non-specific binding of drugs to human liver microsomes and; 5) computationally model the non-specific binding of drugs to discriminate between high binding (fu(mic) less than 0.5) and low binding (fu(mic) greater than 0.5) drugs. The comparative binding of the basic drugs atenolol (log P = 0.1; fu(mic) = 1.00), of propranolol (log P = 3.1; fu(mic) = 0.36 - 0.84), and imipramine (log P = 4.8; fu(mic) = 0.42 - 0.82) suggested that lipophilicity is a major determinant of non-specific binding. In contrast, the comparative binding of diazepam (pKa = 3.3; fu(mic) = 0.69 - 0.80), a neutral compound; and the bases propranolol (pKa = 9.5; fu(mic) = 0.36 - 0.84) and lignocaine (pKa = 9.5; fu(mic) = 0.98), indicated that pKa was not a determinant of the extent of non-specific binding. The non-binding of lignocaine, a relatively lipophilic base, was unexpected and confirmed by the non-binding of the structurally related compounds bupivacaine and ropivacaine. These results implicated physicochemical characteristics other than lipophilicity and charge as important for the non-specific binding of drugs to human liver microsomes. An assay based on 1-anilinonaphthalene-8-sulfonate (ANS) fluorescence was developed using the seven drugs employed in the initial study. Non-specific binding data from equilibrium dialysis and the ANS fluorescence methods were compared and a linear correlation (r2 = 0.92, p less than 0.01) was observed at drug concentrations of 100 and 200 micromolar. The approach was further validated by characterising the microsomal binding of nine compounds (bupropion, chloroquine, chlorpromazine, diflunisal, flufenamic acid, meclofenamic acid, mianserine, triflupromazine, and verapamil) using both binding methods (i.e. equilibrium dialysis and ANS fluorescence). A significant logarithmic relationship (r2 greater than or equal to 0.90) was demonstrated between fu(mic) and the modulus of ANS fluorescence for all drugs and for basic drugs alone at concentrations of 100 and 200 micromolar, while the acidic/neutral drugs showed a significant linear relationship (r2 greater than or equal to 0.84) at these two concentrations (p less than 0.01). The non binding of bupropion provided further evidence that physicochemical properties other than log P and charge were important for non-specific binding of drugs to human liver microsomes. The ANS fluorescence technique was then used to characterise the non-specific binding of 88 physicochemically diverse compounds. In general, acids and neutrals bound to a ‘low’ extent (fu(mic) greater than 0.5) whereas bases bound the full fu(mic) range (0.0001 to 1). Statistically significant relationships were observed between the non-specific binding of bases and log P, the number of hydrogen bond donors and hydrogen bond acceptors per molecule, and molecular mass. Preliminary in silico modeling of the dataset generated by the ANS fluorescence technique, using the program ROCS, provided discrimination of all but one (itraconazole) of the ‘high’ binding bases. However, there were 14 false positives, resulting in low overall prediction accuracy. Taken together, the studies conducted in this thesis provide important insights into the physicochemical factors that determine the non-specific binding of drugs to human liver microsomes.
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Schjølberg, Tiril Helgesen. "In Vitro Synthesis of Metabolites of three Anabolic Androgenic Steroids, by Human Liver Microsomes." Thesis, Norges teknisk-naturvitenskapelige universitet, Institutt for bioteknologi, 2013. http://urn.kb.se/resolve?urn=urn:nbn:no:ntnu:diva-22910.

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Anabolic androgenic steroids are substances frequently misused to improve physicalperformance in sports. To reveal substances misused as doping, athlete urinesamples are collected and tested. To identify the steroid and/or its metabolitesin urine, reference compounds must exist for comparison. The time-consumingand ethical concerns about in vivo excretion studies for the examination of thesecompounds, make the use of liver fragment microsomes an attractive alternative.The aim of this thesis was to synthesize and identify metabolites from known andrare anabolic androgenic steroids, by the use of human liver microsomes. Liveris an important organ in steroid metabolism. By incubating AAS with humanliver microsomes and co factors, an in vitro simulation of the liver metabolism wascarried out. A conrmation of metabolites was performed by gas chromatographytandem mass spectrometry in full scan, MRM mode, or both. 6beta-hydroxymethylmetandienon, epimetandienon and 17,17-dimethylmetandienon were successfullysynthesized from metandienon, and the 17beta-hydroxymetandienon was producedfrom the 17,17-dimethyl metabolite. Respectively three and one metabolite(s)were found for the "designer steroids" methylnortestosteron and madol. Metabolitevariations were observed regarding the optimal time of incubation, and enzymaticrequirements of formation.
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Maley, Mary. "The role of individual forms of cytochrome P450 in drug metabolism in human liver microsomes." Thesis, University of Aberdeen, 1996. http://digitool.abdn.ac.uk/R?func=search-advanced-go&find_code1=WSN&request1=AAIU078654.

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Human liver microsomal metabolism of nicardipine was investigated and compared to that of another dihydropyridine, felodipine, and to published results for other compounds belonging to this class of drugs. The metabolism of tamoxifen and two iododerivatives, idoxifene and 4-iodotamoxifen, were also investigated. Nicardipine metabolism by human liver microsomes was dissimilar to that of other dihydropyridines in several respects. For most dihydropyridines studied to date, conversion to the corresponding pyridine is the major metabolic pathway; the results from this study suggested that pyridine formation is not the major pathway of human liver nicardipine metabolism. The oxidation of most dihydropyridines in human liver microsomes is CYP3A-dependent. In this study, the results from correlation studies and inhibition experiments implicated only CYP3A in nicardipine metabolism, however, not to the same extent as for other dihydropyridines. N-demethylation is the major metabolic route for tamoxifen in human liver and is dependent on the activity of CYP3A. The results from this study suggested that CYP3A is not largely involved in the metabolism of idoxifene and 4-iodotamoxifen in human liver microsomes. Incubations of idoxifene with human liver microsomes resulted in the formation of two metabolites, neither of which could be identified. Correlation and inhibition studies indicated that CYP1A, 2C, 2D and 3A were not involved in idoxifene metabolism in human liver microsomes, although, there was some evidence to support CYP2A involvement. Incubation of 4-iodotamoxifen with microsomes resulted in the formation of up to four metabolites, two of which could be identified. The formation of N-desmethyl 4-iodotamoxifen, the second largest metabolite, appeared to be dependent on CYP3A in human liver microsomes. Correlation studies did not implicate any P450 in the other pathways of 4-iodotamoxifen metabolism in human liver microsomes.
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Abu-Omar, Ghada M. "Drug interactions and metabolism of cyclosporin A and steroids by human liver microsomes in vitro." Thesis, University of Aberdeen, 1992. http://digitool.abdn.ac.uk/R?func=search-advanced-go&find_code1=WSN&request1=AAIU545502.

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1) The purpose of this work is to study the enzymology of cyclosporin A (CsA) metabolism by human liver in vitro , in particular investigating the basis for interindividual variations and drug interactions involving CsA metabolism, and to apply this knowledge to the development of a non-invasive test for predicting an individual's ability to metabolise CsA in vivo . The ultimate aim is to help to improve CsA therapy by understanding the factors which determine its metabolism in patients. 2) Human liver microsomes metabolised cyclosporin A (Km 25M) to eight identifiable metabolites, which were detected following incubation with [3H]-CsA in the presence of NADPH and aerobic O2. An interindividual variation in the generation of CsA metabolites was also observed. In addition, the formation rates of primary and secondary CsA metabolites were induced to different extents by 2 and 4 fold respectively, in liver microsomes prepared from patients treated with anticonvulsant treatment. Metabolite M1 formation was also induced by anticonvulsant treatment. 3) A significant correlation was observed between the total rate of CsA metabolism and cytochrome P-450IIIA concentration as measured by Western blot analysis, in 9 human liver microsomal preparations; 6 were obtained from untreated individuals and 3 from anticonvulsant-treated patients. This correlation was also present when the primary and the secondary metabolite profiles were considered separately. The kinetics of CsA metabolism by human liver microsomes demonstrated different Km and Vmax values for the formation rates of primary and secondary CsA metabolites. This suggests the possible involvement of two enzymes within the P-450IIIA family, responsible for the formation of primary and secondary metabolites, respectively. 4) Anti P-450IIIA antibodies inhibited the total rate of CsA metabolism in microsomal preparations from anticonvulsant-treated patients but to a lesser extent than those from untreated individuals. This suggests an involvement of other form(s) of P-450in CsA metabolism, responsible for between 20-30&'37 of CsA metabolic activity in human liver microsomes. However, these are unlikely to be P-450IIB1, P-450IA1 or P-450IIC, as none of the antibodies raised against these P450s significantly inhibited the metabolism of CsA. 5) From induction, inhibition and correlation studies, cytochrome P-450IIIA has been confirmed as being responsible for the major part of CsA metabolism in human and rat liver microsomes.
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Dowsley, Taylor Forbes. "CYP2E1-dependent bioactivation of 1,1-dichloroethylene to reactive intermediates in murine and human lung and liver microsomes." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp02/NQ38304.pdf.

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Strömqvist, Malin. "Development of quantitative methods for the determination of vemurafenib and its metabolites in human plasma." Thesis, Linköpings universitet, Kemi, 2014. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-110076.

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Vemurafenib is a potent serine/threonine kinase inhibitor and is registered as Zelboraf® for the treatment of metastatic melanomas harboring BRAFV600E mutations. There is a large individual variation in drug response and the side effects observed among patients treated with Zelboraf® has proven to be severe.  LC-MS/MS methods were developed to measure vemurafenib and its metabolites in human plasma for prediction of treatment outcome and side effects in order to individualize treatment with Zelboraf®.  A novel, rapid quantification method was developed for vemurafenib using a stable isotope labeled internal standard. The method was validated according to international guidelines with regard to calibration range, accuracy, precision, carry-over, dilution integrity, selectivity, matrix effects, recovery and stability. All parameters met the set acceptance criteria.  The first method suitable for quantifying vemurafenib metabolites in human plasma is presented. Lacking commercially available reference substances, human liver microsomes were used to produce the metabolites. In patient samples at steady-state five previously in vitro identified metabolites were quantified for the first time.
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Shepard, Dale Randall. "The Metabolism of Phenytoin by Human Liver Microsomes and Cytochrome P450s Expressed in Saccharomyces Cerevisiae and COS-1 Cells /." The Ohio State University, 1995. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487931512618872.

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Uwimana, Eric. "Probing the PCB metabolome: metabolism of chiral and non-chiral polychlorinated biphenyls to chiral hydroxylated metabolites in humans and rats." Diss., University of Iowa, 2018. https://ir.uiowa.edu/etd/6657.

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Polychlorinated biphenyls (PCBs) continue to pose a health concern because of their predominance in the diet and air as well as in environmental samples and humans. PCB congeners with 3 or 4 chlorine substituents in ortho position have been associated with neurodevelopmental disorders. Hydroxylated metabolites (OH-PCBs) of these PCBs are also potentially toxic to the developing brain. Metabolism studies have mainly focused on animal models. However, preliminary data from this dissertation work have revealed PCB metabolism differences between laboratory animal models and humans in terms of metabolite profiles, chiral signatures. More concerning, biotransformation of chiral PCBs is poorly investigated in humans. The objective of this dissertation research was to study the biotransformation of chiral and prochiral PCBs to chiral hydroxylated metabolites in humans and rats and to identify individual human P450 enzymes involved in the metabolism of these PCBs. I chose chiral PCB congeners 2,2',3,4',6-pentachlorobiphenyl (PCB 91); 2,2',3,5',6-pentachlorobiphenyl (PCB 95), 2,2',3,3',4,6'-hexachlorobiphenyl (PCB 132) and 2,2',3,3',6,6'-hexachlorobiphenyl (PCB 136) for this investigation because they are environmentally relevant and their metabolism has been studied in rodents and other laboratory animal species (Kania-Korwel et al., 2016a). Prochiral PCB congeners 2,2′,4,6′-tetrachlorobiphenyl (PCB 51) and 2,2′,4,5,6′-pentachlorobiphenyl (PCB 102) were selected because their considerable presence in technical PCB mixtures. To test the hypothesis that P450 enzyme and species differences mediate the congener-specific enantioselective metabolism of chiral PCBs to hydroxylated metabolites, I sought to establish structure-metabolism relationships by studying the enantioselective metabolism of structurally diverse chiral PCBs by human liver microsomes (HLMs). Racemic PCB 91, PCB 95 and PCB 132 were incubated in vitro with pooled or individual donor HLMs at 37 °C, and levels and chiral signatures of the parent PCB and its hydroxylated metabolites were determined by high-resolution gas chromatography equipped with time-of-flight mass spectrometry (GC/TOF-MS) or electron capture detection (GC-ECD). Hydroxylated metabolites formed were identified and metabolic schemes for these PCBs proposed. I found inter-individual differences in the formation of OH-PCBs by individual donor HLMs. Comparison of the metabolite profiles of PCB 91, PCB 95, PCB 132 and PCB 136 (PCB 136 metabolism by HLMs was investigated by other researchers) revealed congener-specific differences in the oxidation of PCBs by human cytochrome P450 enzymes. PCB 91 and PCB 132 were mainly hydroxylated in meta position, with the 1,2-shift metabolites being the major metabolites formed from both PCB congeners by HLMs. In contrast, PCB 95 and PCB 136 were primarily hydroxylated in the para position. Moreover, we determined human P450 isoforms involved in the metabolism of neurotoxic PCBs using in silico and in vitro approaches. In silico predictions suggested that chiral PCBs are metabolized by CYP1A2, CYP2A6, CYP2B6, CYP2E1, and CYP3A4. Experimentally we found that CYP2A6, CYP2B6 and to a minor extent CYP2E1 were the enzymes involved in the metabolism of these chiral PCBS. We also investigated nonchiral sources of chiral OH-PCBs by studying the P450- and species-dependent biotransformation of prochiral PCB 51 and PCB 102 to chiral OH-PCB metabolites. Prochiral PCB 51 and PCB 102 were incubated with liver microsomes prepared from male Sprague-Dawley rats pretreated with various inducers of P450 enzymes including phenobarbital (PB), dexamethasone (DEX), isoniazid (INH), β-naphthoflavone (BNF), clofibric acid (CFA) or corn oil (CO); and untreated male cynomolgus monkeys, Hartley albino guinea pigs, New Zealand rabbits, golden Syrian hamsters; and untreated female Beagle dogs. PCB 51 and PCB 102 were metabolized to 2,2',4,6'-tetrachlorobiphenyl-3'-ol (OH-PCB 51) and 2,2',4,5,6'-pentachlorobiphenyl-3'-ol (OH-PCB 102), respectively. The formation of both metabolites was P450 isoforms- and species-dependent. Moreover, OH-PCB 51 and OH-PCB 102 were chiral and were formed enantioselectively in all microsomes investigated. Taken together, my findings demonstrate (1) considerable inter-individual variability in the congener-specific metabolism of PCBs to OH-PCBs; (2) the enantioselective formation of OH-PCBs by human CYP2A6, CYP2B6, and CYP2E1; and (3) that chiral PCB metabolites are formed enantioselectively from prochiral PCB congeners. Interestingly, the metabolism of PCBs by CYP2A6 appears to involve arene oxide intermediates, as suggested by the formation of 1,2-shift products as major metabolites of PCB 91 and PCB 132. In contrast, 1,2-shift products are minor PCB metabolites formed in rodents. Therefore extrapolation of hepatic metabolism across species may not be consistent and these differences should be considered in future toxicity and risk assessment studies.
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Larabi, Islam Amine. "Nouveaux produits de synthèse : analyse, consommation et métabolisme ; Applications cliniques et médicolégales Rapid and simultaneous screening of new psychoactive substances and conventional drugs of abuse. A comparative study of Biochip Array Technology versus LC-MS/MS in whole blood and urine Development of a sensitive untargeted liquid chromatography– high resolution mass spectrometry screening devoted to hair analysis through a shared MS2 spectra database: A step toward early detection of new psychoactive substances Validation of an UPLC-MS/MS method for the determination of sixteen synthetic cannabinoids in human hair. Application to document chronic use of JWH-122 following a non-fatal overdose Development and validation of liquid chromatography-tandem mass spectrometry targeted screening of 16 fentanyl analogs and U-47700 in hair: Application to 137 authentic samples Prevalence and Surveillance of Synthetic Cathinones Use by Hair Analysis: An Update Review Prevalence of New Psychoactive Substances(NPS) and conventional drugs of abuse (DOA) in high risk populations from Paris(France) and its suburbs A cross sectional study by hair testing(2012–2017) Evaluation of drug abuse by hair analysis and self-reported use among MSM under PrEP: Results from a sub-study of the ANRS-IPERGAY trial. Hair testing for 3‑fluorofentanyl, furanylfentanyl, methoxyacetylfentanyl, carfentanil, acetylfentanyl and fentanyl by LC–MS/MS after unintentional overdose Drug‐facilitated sexual assault (DFSA) involving 4‐methylethcathinone (4‐MEC),3,4‐Methylenedioxypyrovalerone (MDPV), and doxylamine highlighted by hair analysis Metabolic Profiling of Deschloro-N-ethyl-ketamine (O-PCE) and identification of new target metabolites in urine and hair using human liver microsomes and high-resolution accurate mass spectrometry." Thesis, université Paris-Saclay, 2020. http://www.theses.fr/2020UPASL029.

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L’objectif de ce travail a été de développer deux approches analytiques dédiées à l’analyse toxicologique des nouveaux produits de synthèse (NPS) dans différentes matrices biologiques (sang, urine et cheveux). La première est basée sur le criblage non ciblé par chimiluminescence sur biopuces et chromatographie liquide couplée à la spectrométrie de masse haute résolution (LC-HRMS) et la deuxième correspond à un criblage ciblé par spectrométrie de masse en tandem (LC-MS/MS). Ces deux approches ont ensuite été appliquées dans des études observationnelles pour évaluer la consommation de NPS dans des populations à risques de surdosage, de pharmacodépendance ou de soumission chimique dans un contexte clinique ou médico-judiciaire.La dernière partie a été consacrée au développement d’un nouvel outil analytique de traitement des données issues de la LC-HRMS qui a permis d’étudier le métabolisme de 9 NPS in vitro sur des cultures de microsomes du foie humain (HLM) et in vivo sur des échantillons biologiques d’usagers de ces drogues. Cette dernière approche a permis la création d’une bibliothèque de spectres de haute résolution composée de 228 métabolites dont certains ont été proposés comme marqueurs pertinents d’exposition aux NPS dont ils sont issus.Ce travail a été concrétisé par la rédaction de 10 publications scientifiques et a permis d’initier plusieurs collaborations pluridisciplinaires
The aim of the present work was to develop two analytical approaches dedicated to the analysis of new psychoactive substances in different biological matrices (blood, urine and hair). The first approach is based on untargeted screening by both biochip array technology chemiluminescence assay and liquid chromatography coupled to high resolution mass spectrometry (LC-HRMS) and the second corresponds to a targeted screening by liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS). These two approaches were then applied in observational studies to assess the consumption of NPS in high risk populations (overdose, drug abuse, drug facilitated crimes) in clinical and forensic settings. The last part of the work was devoted to the development of a new analytical tool for LC-HRMS data processing which made it possible to study the metabolism of 9 NPS In vitro on human liver microsomes (HLM) and In vivo in biological samples from drug users. This approach has enabled the creation of HRMS spectral library containing 228 metabolites, some of which have been proposed as relevant markers of NPS exposure.This work has resulted on 10 scientific publications and allowed to initiate many multidisciplinary collaborations
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Books on the topic "Human liver microsomes"

1

Nicotine C-oxidation by human liver microsomes: A major role for CYP2A6. Ottawa: National Library of Canada, 1996.

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Barsoum, Rashad S. Schistosomiasis. Edited by Neil Sheerin. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0181_update_001.

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AbstractSchistosomes are blood flukes that parasitize humans, apes, cattle, and other animals. In these definitive hosts they are bisexual, and lay eggs which are shed to fresh water where they complete an asexual cycle in different snails, ending in the release of cercariae which infect the definitive hosts to complete the life cycle.Seven of over 100 species of schistosomes are human pathogens, causing disease in different organs depending on the parasite species. Racial and genetic factors are involved in susceptibility, severity, and sequelae of infection.Morbidity is induced by the host’s immune response to schistosomal antigens. The latter include tegument, microsomal, gut, and oval antigens. The former are important in the process of invasion and establishment of infection, oval antigens in formation of granulomata which lead to fibrosis in different sites, and the gut antigens constitute the main circulating antigens in established infection, leading to immune-complex disease, particularly in the kidneys. The host immunological response includes innate and adaptive mechanisms, the former being the front line responsible for removing 90% of the infecting cercarial load. Adaptive immunity includes a Th1 phase, dominated by activation of an acute inflammatory response, followed by a prolonged Th2 phase which is responsible for immunity to re-infection as well as progression of tissue injury. Switching from Th1 to Th2 phases is controlled by functional and morphological change in the antigen-presenting cells, which is achieved by molecules of host as well as parasitic origin.Many cells participate in parasite killing, but also in the induction of tissue injury. The most potent of these is the eosinophil, which by binding antibodies to the parasite, particularly immunoglobulin E, facilitates parasite elimination. However, this process is complex, including agonist as well as antagonist pathways, which provide escape mechanisms for the parasite to survive, thereby achieving a delicate balance that permits schistosomes to live for decades in the infected host.
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Book chapters on the topic "Human liver microsomes"

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McManus, M. E., D. J. Birkett, W. M. Burgess, I. Stupans, J. A. Koenig, A. R. Boobis, D. S. Davies, P. J. Wirth, P. H. Grantham, and S. S. Thorgeirsson. "Flavin-Containing Monooxygenase Activity in Human Liver Microsomes." In Biological Reactive Intermediates III, 773–79. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5134-4_72.

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Jia, Jia. "Cytochrome P450 Inhibition Assay Using Human Liver Microsomes." In Methods in Pharmacology and Toxicology, 91–105. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1542-3_6.

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Yan, Zhengyin, and Gary W. Caldwell. "Evaluation of Cytochrome P450 Inhibition in Human Liver Microsomes." In Optimization in Drug Discovery, 231–44. Totowa, NJ: Humana Press, 2004. http://dx.doi.org/10.1385/1-59259-800-5:231.

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Coe, Kevin J., Judith Skaptason, and Tatiana Koudriakova. "Identification of Time-Dependent CYP Inhibitors Using Human Liver Microsomes (HLM)." In Methods in Pharmacology and Toxicology, 305–14. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-742-6_18.

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Wu, Wu-Nan, and Linda A. McKown. "In Vitro Drug Metabolite Profiling Using Hepatic S9 and Human Liver Microsomes." In Optimization in Drug Discovery, 163–84. Totowa, NJ: Humana Press, 2004. http://dx.doi.org/10.1385/1-59259-800-5:163.

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Christians, U., H. M. Schiebel, J. Bleck, and K. Fr Sewing. "Elucidation of the Metabolic Pathways of Cyclosporine in Vitro by Human Liver Microsomes." In Drugs and the Liver: High Risk Patients and Transplantation, 165–70. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1994-8_27.

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Benga, Gh. "Molecular Composition, Fluidity of Membranes and Functional Properties of Human Liver Mitochondria and Microsomes." In Molecular Basis of Membrane-Associated Diseases, 285–302. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-74415-0_24.

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Hörnsten, Lena, Johan Bylund, and Ernst H. Oliw. "Bisallylic Hydroxylation of Linoleic and Arachidonic Acids by Adult and Fetal Human Liver Microsomes and a Comparison with Human Recombinant Cytochromes P450." In Advances in Experimental Medicine and Biology, 123–26. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4899-1810-9_25.

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Caldwell, Gary W., and Zhengyin Yan. "Rapidly Distinguishing Reversible and Time-Dependent CYP450 Inhibition Using Human Liver Microsomes, Co-incubation, and Continuous Fluorometric Kinetic Analyses." In Methods in Pharmacology and Toxicology, 281–303. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-742-6_17.

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Ahmed, S. Sohail, Kimberly L. Napoli, and Henry W. Strobel. "Oxygen Radical Formation Due to the Effect of Varying Hydrogen Ion Concentrations on Cytochrome P450-Catalyzed Cyclosporine Metabolism in Rat and Human Liver Microsomes." In Advances in Experimental Medicine and Biology, 135–39. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4757-9480-9_19.

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Conference papers on the topic "Human liver microsomes"

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Widdison, Wayne C., Sharon Wilhelm, Karen Veale, Yelena Kovtun, Hans Erickson, Charlene Audette, Barbara Leeca, Gregory Jones, and Ravi Chari. "Abstract 2668: Detoxification of metabolites from antibody-maytansinoid conjugates by human liver microsomes." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2668.

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Liu, Xing, Albert DeJesus, Dana Vardeman, Zhisong Cao, and Beppino Giovanella. "Abstract 4337:In vitrobiotransformation of and inhibitory effects of CZ48 in human liver microsomes." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4337.

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Grafakou, M. E., C. Barda, E. Skaltsa, and J. Heilmann. "Identification of parthenolide metabolites in human liver microsomes by LC-Q-TOF-MS/MS." In GA – 69th Annual Meeting 2021, Virtual conference. Georg Thieme Verlag, 2021. http://dx.doi.org/10.1055/s-0041-1736874.

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Ouyang, Hui, Huiping Liao, Junmao Li, Mingzhen He, Yan Li, Xiaoyong Rao, Qi Wang, Shilin Yang, Zhifeng Li, and Yulin Feng. "COMPARATIVE METABOLISM CHARACTERISTICS RESEARCH OF TETRAHYDROPALMATINE IN FIVE SPECIES (DOG, HUMAN, MICE, MONKEY, AND RAT) LIVER MICROSOMES BY UHPLC/ESI-QTOF-MS/MS." In 2016 International Conference on Biotechnology and Medical Science. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789813145870_0023.

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Reports on the topic "Human liver microsomes"

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Abou-Donia, M. B., and A. W. Abu-Quare. In Vitro Metabolism of Pyridostigmine Bromide (PB), DEET and Permethrin, Alone and in Combination by Human Plasma and Liver Microsomes. Fort Belvoir, VA: Defense Technical Information Center, March 2001. http://dx.doi.org/10.21236/ada402080.

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Casabar, Richard C., Andrew D. Wallace, Ernest Hodgson, and Randy L. Rose. Metabolism of Endosulfan-Alpha by Human Liver Microsomes and its Utility as a Simultaneous In Vitro Probe for CYP2B6 and CYP3A4. Fort Belvoir, VA: Defense Technical Information Center, March 2006. http://dx.doi.org/10.21236/ada445178.

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