Article (Scientific journals)
Is steroid 16alpha-hydroxylase supported by more than one mono-oxygenase.
Kremers, Pierre; Pasleau, Françoise; Gielen, Jacques
1978In Biochemical and Biophysical Research Communications
Peer reviewed
 

Files


Full Text
P. Kremers - Biochem. & Biophys. Res. Commun. - 1978.pdf
Publisher postprint (343.77 kB)
Request a copy

All documents in ORBi are protected by a user license.

Send to



Details



Abstract :
[en] Steroid-16α-hydroxylase activities have been measured in normal and induced rat livers using four different substrates. The male/female activity ratio as well as the induction factor vary with the substrate indicating that steroid-16α-hydroxylase activity is a heterogenous enzyme. Experiments using specific inhibitors led to the conclusion that steroid-16α-hydroxylase is supported by at least two cytochrome P-450 forms, different from the cytochrome P-448.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Kremers, Pierre ;  Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences)
Pasleau, Françoise ;  Université de Liège - ULiège > CARE "Le Réseau des bibliothèques" > Bibliothèque des Sciences de la vie
Gielen, Jacques
Language :
English
Title :
Is steroid 16alpha-hydroxylase supported by more than one mono-oxygenase.
Publication date :
16 October 1978
Journal title :
Biochemical and Biophysical Research Communications
ISSN :
0006-291X
eISSN :
1090-2104
Publisher :
Academic Press (part of Elsevier), San Diego, United States
Peer reviewed :
Peer reviewed
Available on ORBi :
since 09 July 2009

Statistics


Number of views
54 (7 by ULiège)
Number of downloads
0 (0 by ULiège)

Bibliography


Similar publications



Contact ORBi