DMD Simcyp

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Shih, T. W.
Right arrow Articles by Hill, D. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shih, T. W.
Right arrow Articles by Hill, D. L.

Conversion of retinol to retinal by rat liver microsomes

TW Shih and DL Hill

Southern Research Institute, Birmingham, AL 35255-5305.

An NADPH-requiring enzyme present in rat liver microsomes catalyzes the conversion of retinol to retinal; the enzyme activity is induced by 3- methylcholanthrene (MC). The optimum activities for both the constitutive and induced reactions occur within a pH range of 8.2-8.7. For the constitutive enzyme, the KM and Vmax values are 285 microM retinol and 18 nmol of retinal/mg protein/hr, respectively; for the MC- induced activity, the corresponding values are 133 microM retinol and 33 nmol of retinal/mg protein/hr. Neither the constitutive nor the induced activities are detectable in microsomes from seven other tissues. Both hepatic activities are inhibited by citral, ketoconazole, SKF 525-A, and alpha-naphthoflavone; both are stimulated by divalent cations. Neither is inhibited by 3-amino-1,2,4-triazole, pyrazole, or sodium azide or stimulated by monovalent cations. The enzyme appears to be a previously unreported retinol oxidase, distinct from the known cytosolic enzymes, retinal reductase and retinol dehydrogenase.

Volume 19, Issue 2, pp. 332-335, 03/01/1991
Copyright © 1991 by American Society for Pharmacology and Experimental Therapeutics




This article has been cited by other articles:


Home page
 Drug Metab. Dispos.Home page
H. Chen, W. N. Howald, and M. R. Juchau
Biosynthesis Of All-trans-Retinoic Acid from All-trans-Retinol: Catalysis of All-trans-Retinol Oxidation by Human P-450 Cytochromes
Drug Metab. Dispos., March 1, 2000; 28(3): 315 - 322.
[Abstract] [Full Text] [PDF]

Home page
 CLIN APPL THROMB HEMOSTHome page
T. W. Stief and J. Fareed
State-of-the-Art-Review : The Antithrombotic Factor Singlet Oxygen/Light (1O2/hv)
Clinical and Applied Thrombosis/Hemostasis, January 1, 2000; 6(1): 22 - 30.
[Abstract] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
All ASPET Journals Molecular Pharmacology Pharmacological Reviews
Molecular Interventions Drug Metabolism and Disposition

Copyright © 1991 by the American Society for Pharmacology and Experimental Therapeutics.