Reduction kinetics of purified rat liver cytochrome P-450. Evidence for a sequential reaction mechanism dependent on the hemoprotein spin state

Biochemistry ◽  
1984 ◽  
Vol 23 (20) ◽  
pp. 4526-4533 ◽  
Author(s):  
Paul P. Tamburini ◽  
G. Gordon Gibson ◽  
Wayne L. Backes ◽  
Stephen G. Sligar ◽  
John B. Schenkman
Author(s):  
J. O. Stern ◽  
E. Peisach ◽  
J. Peisach ◽  
W. E. Blumberg ◽  
A. Y. H. Lu ◽  
...  

Abstracts ◽  
1978 ◽  
pp. 289
Author(s):  
Thierry CRESTEIL ◽  
Philippe BEAUNE ◽  
Jean-Paul LEROUX

1978 ◽  
Vol 172 (3) ◽  
pp. 417-422 ◽  
Author(s):  
E E Delvin ◽  
A Arabian ◽  
F H Glorieux

Kinetics of vitamin D-depleted and -repleted rat liver microsomal cholecalciferol 25-hydroxylase were studied. Anaerobiosis, CO, omission of a NADPH-generating system and addition of detergents all decreased the activities, showing that the hydroxylase behaves like a cytochrome P-450-dependent enzyme. An apparent Km of 0.18 micrometer and Vmax. of 32pmol/min per g of tissue were found for vitamin D-deficient animals. Although both apparent Km and Vmax. were significantly altered in vitamin D-repleted animals no inhibition of the enzyme was elicited. These latter results show that at normal vitamin D intake, rat liver cholecalciferol 25-hydroxylase is not feedback-inhibited.


Xenobiotica ◽  
1992 ◽  
Vol 22 (5) ◽  
pp. 515-522 ◽  
Author(s):  
G. J. M. Horbach ◽  
J. G. Van Asten ◽  
I. M. C. M. Rietjens ◽  
P. Kremers ◽  
C. F. A. Van Bezooijen

1983 ◽  
Vol 32 (15) ◽  
pp. 2309-2318 ◽  
Author(s):  
Marcel Delaforge ◽  
Maryse Jaouen ◽  
Daniel Mansuy

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