![]()
|
|
||||||||
From the
1 From the Departments of Biochemistry and Medicine, University of Southern California School of Medicine, Los Angeles, California 90053
Difference spectra of mitochondrial and microsomal preparations from bovine adrenal cortex have been examined, and the activity of several enzyme systems in these particles has been studied. Evidence for nicotinamide adenine dinucleotide, flavoproteins, and cytochromes b, c1, c, and a + a3 in the adrenal respiratory chain in a molar ratio of 4.9:3.8:1.7:1.5:2.0:2.9:1.0, respectively, was found. The P-450 cytochrome was observed to be present in mitochondria in a molar ratio to cytochrome a3 of 6.9:1.0. It paralleled malate oxidase and steroid 11ß-hydroxylase activities in subcellular distribution but was also present at a lower concentration in microsomal particles which contained most of the steroid 21-hydroxylase activity. The relationship of the adrenal cortical respiratory chain to the mitochondrial steroid-hydroxylating pathway is discussed, and a role for an energy-controlled pyridine nucleotide transhydrogenase in electron transport to the hydroxylating system is suggested.
Electron Carriers of the Bovine Adrenal Cortical Respiratory Chain and Hydroxylating Pathways
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
D. W. Shoeman, J. G. White, and G. J. Mannering Cytochrome P-420: Tubular Aggregates from Hepatic Microsomes Science, September 26, 1969; 165(3900): 1371 - 1372. [Abstract] [PDF] |
||||
![]() |
C. J. Sih Enzymatic Mechanism of Steroid Hydroxylation Science, March 21, 1969; 163(3873): 1297 - 1300. [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |