Production of Carbon Monoxide by Sonication of Medium Containing Glycerol. Effect on Cytochrome P-450 Reconstituted Systems

1982 ◽  
pp. 377-380
Author(s):  
V. Luu-The ◽  
Ch. Vandresse ◽  
J. Cumps ◽  
P. Dumont
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome P 450

Oxygenation of 18-hydroxycorticosterone as the final reaction for aldosterone biosynthesis

1984 ◽  
Vol 107 (3) ◽  
pp. 395-400 ◽  
Author(s):  
Itaru Kojima ◽  
Etsuro Ogata ◽  
Hiroshi Inano ◽  
Bun-ichi Tamaoki
Keyword(s):  
Carbon Monoxide ◽  
Hydroxysteroid Dehydrogenase ◽  
Dependent Manner ◽  
In Vitro Production ◽  
Mitochondrial Preparation ◽  
Final Reaction ◽  
Vitro Production ◽  
Dose Dependent ◽  
Cytochrome P 450

Abstract. Incubation of 18-hydroxycorticosterone with the sonicated mitochondrial preparation of bovine adrenal glomerulosa tissue leads to the production of aldosterone, as measured by radioimmunoassay. The in vitro production of aldosterone from 18-hydroxycorticosterone requires both molecular oxygen and NADPH, and is inhibited by carbon monoxide. Cytochrome P-450 inhibitors such as metyrapone, SU 8000. SU 10603, SKF 525A, amphenone B and spironolactone decrease the biosynthesis of aldosterone from 18-hydroxycorticosterone. These results support the conclusion that the final reaction in aldosterone synthesis from 18-hydroxycorticosterone is catalyzed by an oxygenase, but not by 18-hydroxysteroid dehydrogenase. By the same preparation, the production of [3H]aldosterone but not [3H]18-hydroxycorticosterone from [1,2-3H ]corticosterone is decreased in a dose-dependent manner by addition of non-radioactive 18-hydroxycorticosterone.

SOME CHEMICAL PROPERTIES OF CYTOCHROME P-450 AND ITS CARBON MONOXIDE COMPOUND (P-450.CO)

1970 ◽  
Vol 174 (1 Biological Ef) ◽  
pp. 205-217 ◽  
Author(s):  
David Y. Cooper ◽  
Heinz Schleyer ◽  
Dr. rer. Nat ◽  
Otto Rosenthal
Keyword(s):  
Carbon Monoxide ◽  
Chemical Properties ◽  
Cytochrome P 450

Formation of similar species to carbon monoxide during hepatic microsomal metabolism of cannabidiol on the basis of spectral interaction with cytochrome P-450

1988 ◽  
Vol 37 (24) ◽  
pp. 4719-4726 ◽  
Author(s):  
Watanabe Kazuhito ◽  
Narimatsu Shiuo ◽  
Gohda Hiroshi ◽  
Yamamoto Ikuo ◽  
Yoshimura Hidetoshi
Keyword(s):  
Carbon Monoxide ◽  
Similar Species ◽  
Microsomal Metabolism ◽  
Cytochrome P 450

Ductus arteriosus: involvement of a sarcolemmal cytochrome P-450 in O2 constriction?

1989 ◽  
Vol 67 (11) ◽  
pp. 1448-1450 ◽  
Author(s):  
Flavio Coceani ◽  
Julie Wright ◽  
Carole Breen
Keyword(s):  
Carbon Monoxide ◽  
Ductus Arteriosus ◽  
Signal Transducer ◽  
Mixture Ratio ◽  
Skinned Muscle ◽  
Sequence Of Events ◽  
Membrane Bound ◽  
Cytochrome P 450 ◽  
Constrictor Response ◽  
Insight Into

Our previous studies implicate a cytochrome P-450-based mechanism in the constrictor response of the ductus arteriosus to oxygen. The present experiments were conducted on saponin-skinned strips of ductal muscle from mature fetal lambs to determine the location, sarcolemmal versus intracellular, of this cytochrome and to obtain a better insight into the sequence of events underlying the action of oxygen. Skinned preparations contracted to free Ca2+ over the range between 0.1 and 5–10 μM (pCa 7 to 5). In contrast, oxygen (Po2, 608–690 Torr; 1 Torr = 133.3 Pa) had no significant effect, both in the absence and presence of 10 μM calcium. Carbon monoxide, tested as pure CO or a CO–O2 mixture (ratio 0.28), did not relax preparations maximally contracted with calcium. These findings indicate that oxygen exerts its effect on the plasma membrane of ductus muscle cells and that a membrane-bound cytochrome P-450 mechanism likely functions as the signal transducer for oxygen in the formation of a constrictor agent.Key words: ductus arteriosus closure, chemically skinned muscle, second messenger.

Adrenal cortical cytochrome P-450. III. Effects of carbon monoxide and light on steroid 11β hydroxylation

Biochemistry ◽  
1970 ◽  
Vol 9 (7) ◽  
pp. 1615-1621 ◽  
Author(s):  
Lowell Dean Wilson ◽  
Boyd W. Harding
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome P 450

scholarly journals Loss of haem from cytochrome P-450 caused by lipid peroxidation and 2-allyl-2-isoprophylacetamide. An abnormal pathway not involving production of carbon monoxide

1977 ◽  
Vol 168 (3) ◽  
pp. 417-422 ◽  
Author(s):  
F De Matteis ◽  
A H Gibbs ◽  
A Unseld
Keyword(s):  
Lipid Peroxidation ◽  
Carbon Monoxide ◽  
Significant Extent ◽  
Haem Oxygenase ◽  
Bridge Carbon ◽  
Cytochrome P 450

1. Microsomal preparations undergoing lipid peroxidation produce CO and lose haem from cytochrome P-450. 2. The amount of CO produced does not correlate with the amount of haem lost and, after pre-labelling of microsomal haem in its bridges with 5-amino[5-14C]laevulinate, the radioactivity lost from haem is not recorved as CO. 3. Similarly, when pre-labelled microsomal haem is destroyed by the action of 2-allyl-2-isopropylacetamide, no radioactivity is recovered as CO. In clear contrast, on degradation of haem by the haem oxygenase system, CO is produced in an amount equimolar to the haem lost. 4. It is concluded that (a) the CO produced during lipid peroxidation originates from a source different from haem and (b) the degradations of haem caused by lipid peroxidation and 2-allyl-2-isopropylacetamide do not involve to any significant extent evolution of the methene-bridge carbon of haem as CO.

Interactions of steroids with human placental cytochrome P-450 in the presence of carbon monoxide

Life Sciences ◽  
1975 ◽  
Vol 16 (11) ◽  
pp. 1689-1692 ◽  
Author(s):  
Prince K. Zachariah ◽  
Mont R. Juchau
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome P 450
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