Inactivation of glutamine synthetase by a purified rabbit liver microsomal cytochrome P-450 system
- 1 July 1985
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 240 (1), 319-329
- https://doi.org/10.1016/0003-9861(85)90037-2
Abstract
No abstract availableThis publication has 36 references indexed in Scilit:
- Oxygen Activation by Cytochrome P-4501Annual Review of Biochemistry, 1980
- Intracellular production of superoxide radical and of hydrogen peroxide by redox active compoundsArchives of Biochemistry and Biophysics, 1979
- Properties of NADPH-cytochrome P-450 reductase purified from rabbit liver microsomesArchives of Biochemistry and Biophysics, 1979
- Enzymic procedures for determining the average state of adenylylation of Escherichia coli glutamine synthetaseAnalytical Biochemistry, 1979
- Hydrogen peroxide formation and stoichiometry of hydroxylation reactions catalyzed by highly purified liver microsomal cytochrome P-450Archives of Biochemistry and Biophysics, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Zinc-induced paracrystalline aggregation of glutamine synthetaseArchives of Biochemistry and Biophysics, 1974
- Hepatic Microsomal Ethanol OxidationEuropean Journal of Biochemistry, 1972
- The Carbon Monoxide-binding Pigment of Liver MicrosomesJournal of Biological Chemistry, 1964
- ASCORBIC ACID IN AROMATIC HYDROXYLATIONJournal of Biological Chemistry, 1954