|
|
|
|
Molecular Pharmacology, Vol 3, 516-525, Copyright © 1967 by the American Society for Pharmacology and Experimental Therapeutics
1 Department of Biophysics and Physical Biochemistry, Johnson Research Foundation,
University of Pennsylvania, Philadelphia 19104 and Institut für Toxikologie,
Universität Tübingen, Tübingen, Germany
Sex differences in drug oxidase activity of liver microsomes from rats have been shown to be related to a difference in substrate affinity for the mixed function oxidase reaction, and not to a difference in the content of cytochrome P-450. These results, as well as spectral studies of substrate interaction with microsomal cytochrome, showed that microsomes isolated from livers of male rats had over twice the magnitude of substrate (hexobarbital and aminopyrine) binding than did microsomes isolated from the livers of female rats. Similar studies with aniline indicated only a small difference in Vmax or substrate induced spectral change between microsomes isolated from livers of male or female rats.
Note:
ACKNOWLEDGMENTS
This work was supported in part by a grant
from the National Science Foundation (GB 2451)
and grants from the U.S. Public Health Service
(GM 12202-02 and GM 27706), and by the
Deutsche Forschungsgemeinschaft.
This article has been cited by other articles:
![]() |
M. B. Schabath, M. R. Spitz, X. Zhang, G. L. Delclos, and X. Wu Genetic variants of myeloperoxidase and lung cancer risk Carcinogenesis, June 1, 2000; 21(6): 1163 - 1166. [Abstract] [Full Text] [PDF] |
||||