Rapid determination of six metabolites from multiple cytochrome P450 probe substrates in human liver microsome
by liquid chromatography/mass spectrometry: application to high-throughput inhibition screening of terpenoids.
Lonzas Silensomes HLM products include seven cryopreserved human liver microsomes
pools that are each pre-treated with a mechanistic-based inhibitor targeting a single CYP enzyme.
The objectives of the present study included (1) to identify through ultra-high-performance liquid chromatography/quadrupole time-of-flight mass spectrometry (UPLC/Q-TOF MS) and high-performance liquid chromatography-solid-phase extraction-nuclear magnetic resonance spectroscopy (HPLC-SPE-NMR) the WEL metabolites formed in rats following an oral administration of 50 mg/kg WEL; (2) to determine the uridine diphosphate-glucuronosyltransferases (UGTs) responsible for WEL glucuronidation using human liver microsomes
(HLMs), human intestine microsomes (HIMs), human kidney microsomes (HKMs), and recombinant human UGT enzymes; and (3) to explore the possible mechanisms of WEL regioselective glucuronidation.
Pooled human liver microsomes
(HLMs) were purchased from XenoTech (Kansas, USA).
The effect of gene polymorphisms on SRL metabolism was investigated in vitro using human liver microsomes
, and potential associations with SRL blood concentrations and AEs were explored in parallel in 113 kidney transplant recipients.
In vitro metabolism of midazolam, triazolam, nifedipine, and testosterone by human liver microsomes
and recombinant cytochromes p450: role of cyp3a4 and cyp3a5.
Although toxicokinetic information on TDCPP and TPP is limited, studies using rat and human liver microsomes
suggest that TDCPP and TPP are metabolized rapidly to diesters (e.
Evidence for cytochrome P450 2A6 and 3A4 as major catalysts for N'-nitrosonornicotine a-hydroxylation in human liver microsomes
Purpose: Potential drug-interactions with MA via inhibition of cytochrome P450 (CYP) activity in human liver microsomes
(HLMs), have not been investigated.
OBJECTIVES: The purposes of this study were to characterize the in vitro metabolism of 2,2',4,4'-tetrabromodiphenyl ether (BDE-47) by human liver microsomes
(HLM) and recombinant human CYPs, and to identify the CYP(s) that are active in the oxidative metabolism of BDE-47.
We therefore set out to assess the relative contributions of CYP3A5 and CYP3A4 to the formation of the main tacrolimus metabolite (13-O-demethyltacrolimus), using cDNA-expressed enzymes and a bank of human liver microsomes
derived from low and high CYP3A5 expressers.