Cytochrome P-450 and related components of the microsomal electron transport system in the bovine ciliary body
- 1 January 1986
- journal article
- research article
- Published by Taylor & Francis in Current Eye Research
- Vol. 5 (7) , 529-533
- https://doi.org/10.3109/02713688608996376
Abstract
Microsomes were prepared from bovine ciliary bodies. The contents of cytochrome P-450 and related components of the microsomal electron transport system were determined. The cytochrome P-450 content was 32 pmoles/mg protein, which was about 4% that in rat liver. The cytochrome b5 content was 59 pmoles/mg protein. The NADH-cyto−chrome c reductase and NADPH-cytochrome c reductase activities were 268 and 18 nmoles/min/mg protein, respectively. The ethoxyresorufin deethyl-ase activity was 2.1 pmoles product formed/min/mg protein.This publication has 13 references indexed in Scilit:
- Dealkylation of pentoxyresorufin: A rapid and sensitive assay for measuring induction of cytochrome(s) P-450 by phenobarbital and other xenobiotics in the ratArchives of Biochemistry and Biophysics, 1985
- Enzymes of mercapturate synthesis and other drug-metabolizing reactions-specific localization in the eyeExperimental Eye Research, 1981
- Metabolism of benzo(a)pyrene in bovine lens epitheliumExperimental Eye Research, 1981
- Genetic Mechanisms Controlling the Induction of Polysubstrate Monooxygenase (P-450) ActivitiesAnnual Review of Pharmacology and Toxicology, 1981
- Species and strain differences in target organ alkylation and toxicity by 4-ipomeanolBiochemical Pharmacology, 1979
- Electron spin resonance of microsomal cytochromesArchives of Biochemistry and Biophysics, 1967
- The Carbon Monoxide-binding Pigment of Liver MicrosomesJournal of Biological Chemistry, 1964
- Hepatic Triphosphopyridine Nucleotide-Cytochrome c Reductase: Isolation, Characterization, and Kinetic StudiesJournal of Biological Chemistry, 1962
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951