Show/Hide Menu
Hide/Show Apps
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
Open Access Guideline
Open Access Guideline
Postgraduate Thesis Guideline
Postgraduate Thesis Guideline
Communities & Collections
Communities & Collections
Help
Help
Frequently Asked Questions
Frequently Asked Questions
Guides
Guides
Thesis submission
Thesis submission
MS without thesis term project submission
MS without thesis term project submission
Publication submission with DOI
Publication submission with DOI
Publication submission
Publication submission
Supporting Information
Supporting Information
General Information
General Information
Copyright, Embargo and License
Copyright, Embargo and License
Contact us
Contact us
Effects of 2-arylbenzimidazoles on rat hepatic microsomal monooxygenase system
Date
1989-1
Author
İşcan, Mesude Y.
Büyükbingöl, Erdem
İşcan, Mümtaz
Şahin, Fethi
Şafak, Cihat
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
158
views
0
downloads
Cite This
1. The effects of eight newly synthesized 2-aryl substituted benzimidazole derivatives on control and phenobarbital (PB) treated rat liver microsomal aniline 4-hydroxylase and ethylmorphine N-demethylase activities, and their binding to control and PB-treated rat liver microsomal oxidized cytochrome P-450 are presented. 2. All compounds inhibited ethylmorphine N-demethylase activity with I50 values ranging from 8.50 × 10−4 M to 27.83 × 10−4 M in control and ranging from 2.80 × 10−4 M to 15.79 × 10−4 M in PB-treated rats. 3. Aniline 4-hydroxylase activity was inhibited by all of the compounds tested having I50 values in the range of 7.04 × 10−4 M-31.37 × 10−4 M in PB-treated rats, but only five of the compounds showed inhibitory activity in control rats. 4. Only a few significant regression coefficients could be found between the parameters of the chemicals studied and their inhibitory patterns. 5. No correlation has been observed between the binding of the derivatives and their inhibitory pattern.
Subject Keywords
Immunology
,
Pharmacology
,
Biochemistry and Molecular Biology
,
Endocrinology and Metabolism
,
Toxicology
,
Zoology
URI
https://hdl.handle.net/11511/51733
Journal
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology
DOI
https://doi.org/10.1016/0742-8413(89)90211-9
Collections
Department of Biology, Article
Suggestions
OpenMETU
Core
EFFECTS OF INVIVO BENZENE TREATMENT ON CYTOCHROME-P450 AND MIXED-FUNCTION OXIDASE ACTIVITIES OF GILTHEAD SEABREAM (SPARUS-AURATA) LIVER-MICROSOMES
ARINC, E; SEN, A (Elsevier BV, 1993-01-01)
1. Treatment of gilthead seabream (Sparus aurata) with benzene 0.6 ml/kg/day, s.c., for four consecutive days resulted in a marked 78% and 73% decrease in total cytochrome P450 content and 7-ethoxyresorufin O-deethylase activity of liver microsomes, respectively.
A Comparative Study for the Evaluation of Two Doses of Ellagic Acid on Hepatic Drug Metabolizing and Antioxidant Enzymes in the Rat
Celik, Gurbet; SEMİZ, ASLI; Karakurt, Serdar; ARSLAN, ŞEVKİ; Adalı, Orhan; ŞEN, ALAATTİN (Hindawi Limited, 2013-01-01)
The present study was designed to evaluate different doses of ellagic acid (EA) in vivo in rats for its potential to modulate hepatic phases I, II, and antioxidant enzymes. EA (10 or 30 mg/kg/day, intragastrically) was administered for 14 consecutive days, and activity, protein, and mRNA levels were determined. Although the cytochrome P450 (CYP) 2B and CYP2E enzyme activities were decreased significantly, the activities of all other enzymes were unchanged with the 10 mg/kg/day EA. In addition, western-blot ...
The effect of cysteine-43 mutation on thermostability and kinetic properties of citrate synthase from Thermoplasma acidophilum
Kocabıyık, Semra; Russel, RJM; Danson, MJ; Hough, DW (Elsevier BV, 1996-07-05)
In this study, we have substituted serine-43 by cysteine in the recombinant citrate synthase from a moderately thermophilic Archaeon Thermoplasma acidophilum, for site-specific attachment of labels and have investigated the effects of this mutation on the biochemical properties and thermal stability of the enzyme. Both wild-type and the mutant enzymes were purified to homogenity using affinity chromatography on Matrex Gel Red A. The mutant Thermoplasma citrate synthase is very similar to wild-type citrate s...
Effect of arachidonic acid on specific binding of [H-3]naloxone to opioid receptors
Apaydin, S; Öktem, Hüseyin Avni (2000-01-01)
The effects of arachidonic acid (AA) on binding of [H-3]naloxone to the agonist and antagonist configurations of opioid receptors were investigated in rat brain. Equilibrium binding parameters of the agonist and antagonist configurations of the receptors were evaluated from homologue displacement data in the presence or absence of AA. Addition of AA at a concentration of 0.6 mM (1.5 mu mole/mg of protein) reduced by 22% and 53% the maximal number of binding sites (B-max) respectively in the absence or prese...
Modulation of human flavin-containing monooxygenase 3 activity by tricyclic antidepressants and other agents: Importance of residue 428
Adalı, Orhan; Philpot, RM (Elsevier BV, 1998-10-01)
Human flavin-containing monooxygenase 3 (FMO3) is subject to modulation by tricyclic antidepressants and other agents. Imipramine activates FMO3-catalyzed metabolism of methimazole at all substrate concentrations tested. This distinguishes FMO3 from rabbit FMO1 and FMO2, which are activated at high substrate concentration and inhibited at low substrate concentration, and pig FMO1, which is inhibited at all substrate concentrations. The response of FMO3 is also unique in that chlorpromazine is markedly more ...
Citation Formats
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
M. Y. İşcan, E. Büyükbingöl, M. İşcan, F. Şahin, and C. Şafak, “Effects of 2-arylbenzimidazoles on rat hepatic microsomal monooxygenase system,”
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology
, pp. 109–115, 1989, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/51733.