scholarly journals Effects of bromocriptine on hepatic cytochrome P-450 monooxygenase system.

1989 ◽  
Vol 49 (2) ◽  
pp. 285-291 ◽  
Author(s):  
Shabbir M. MOOCHHALA ◽  
Edmund J.D. LEE ◽  
Gwendolene T.M. HU ◽  
O.S. KOH ◽  
Gordon BECKET
Keyword(s):  
Monooxygenase System ◽  
Cytochrome P 450 ◽  
Hepatic Cytochrome

scholarly journals Effects of Bromocriptine on Hepatic Cytochrome P-450 Monooxygenase System

1989 ◽  
Vol 49 (2) ◽  
pp. 285-291
Author(s):  
Shabbir M. MOOCHHALA ◽  
Edmund J.D. LEE ◽  
Gwendolene T.M. HU ◽  
O.S. KOH ◽  
Gordon BECKET
Keyword(s):  
Monooxygenase System ◽  
Cytochrome P 450 ◽  
Hepatic Cytochrome

scholarly journals Cyclization reactions of IMM-125 and oxidation of cyclosporin A amino-acid 1 in theαposition of the double bond lead to the loss ofin vitroimmunosuppressive activity

2000 ◽  
Vol 14 (4) ◽  
pp. 215-228
Author(s):  
R. Dieden ◽  
D. Latinne ◽  
C. Baldari ◽  
N. Maton ◽  
A. Aubry ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cyclosporin A ◽  
Parent Drug ◽  
Nucleophilic Attack ◽  
Monooxygenase System ◽  
Cyclization Reactions ◽  
Perbenzoic Acid ◽  
Jurkat T Cell ◽  
Cytochrome P 450 ◽  
Hepatic Cytochrome

Cyclosporin A (CsA) and IMM-125, a hydroxyethyl derivative of D-serine CsA, are cyclic undecapeptides of molecular weight 1201.8 and 1261.8, respectively. The main metabolites still possessing the undecapeptide structure were found to be compounds resulting from the biotransformation of amino acids 4, 9 and 1.Under the influence of the hepatic cytochrome P-450-dependent monooxygenase system, CsA and IMM-125 amino acid 1 are metabolized to a mono-hydroxylated compound (metabolite M-17) and to a dihydrodiol. A metabolite M18 was found to be the result of a non-enzymic intramolecular formation of a tetrahydrofuran derivative from metabolite M17. Since the existence of a CsA dihydrodiol was reported and since epoxides are considered as the dihydrodiol precursors, the aim of the present work was to prove that the same non-enzymic intramolecular formation of a tetrahydrofuran ring could occur by nucleophilic attack of the amino-acid 1β-hydroxy group at theɛ-position of the freshly formed epoxide by reaction of IMM-125 with m-chloro-perbenzoic acid and cyclosporin A with selenium oxide. The immunosuppressive activity of the compounds, as measured by the mixed lymphocyte reaction and by the luciferase activity of a Jurkat-T-cell line stably transfected with the NF-AT/luc reporter plasmid, was found negligible for IMM-125 compared to the parent drug as well as for the cyclosporin A derivative. Structures of the IMM-125 and CsA derivatives were elucidated by electrospray mass‒spectrometry and NMR spectroscopy.

scholarly journals Benzobarbital and fluorbenzobarbital - hepatic monooxygenase system phenobarbital-like inducers

2011 ◽  
Vol 10 (5) ◽  
pp. 78-81 ◽  
Author(s):  
T. P. Novozheyeva ◽  
M. I. Smagina ◽  
N. A. Cherevko ◽  
S. N. Fateyeva
Keyword(s):  
Large Degree ◽  
Major Metabolite ◽  
Monooxygenase System ◽  
Oxidation Activity ◽  
Hepatic Monooxygenase ◽  
Cytochrome P 450 ◽  
Hepatic Cytochrome

Benzobarbital and fluorbenzobarbital as monooxygenase system inductors increase the hepatic cytochrome P-450 level and the content of its isoenzymes 2B6, 2C9, 2Å1, accelerate aminopyrine, 7-ethoxyresorufine, 7-pentoxyresorufine, aniline and androstendione oxidation. Activity of benzobarbital and fluorbenzobarbital as inductors is to a large degree due to the action of their major metabolite — phenobarbital. Benzobarbital and fluorbenzobarbital unlike phenobarbital induce isoenzyme 3A4, responsible for androstendione 16b-OH-hydroxylation. PCN-type induction activity posses also native molecules of benzobarbital and fluorbenzobarbital.

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