SPECIFICITY OF RABBIT PULMONARY CYTOCHROME-P-450 ISOZYMES IN THE ACTIVATION OF SEVERAL AROMATIC-AMINES AND AFLATOXIN-B1
- 1 January 1981
- journal article
- research article
- Vol. 20 (3) , 662-668
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- ACETYLORNITHINASE OF ESCHERICHIA COLI: PARTIAL PURIFICATION AND SOME PROPERTIESPublished by Elsevier ,2021
- The rabbit pulmonary monooxygenase system. Immunochemical and biochemical characterization of enzyme components.Journal of Biological Chemistry, 1979
- The role of cytochrome P-450 forms in 2-aminoanthracene and benz[α]pyrene mutagenesisBiochemical and Biophysical Research Communications, 1979
- The rabbit pulmonary monooxygenase system. Catalytic differences between two purified forms of cytochrome P-450 in the metabolism of benzo(a)pyrene.Journal of Biological Chemistry, 1979
- The rabbit pulmonary monooxygenase system: Characteristics and activities of two forms of pulmonary cytochrome P-450Chemico-Biological Interactions, 1978
- Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450Journal of Biological Chemistry, 1976
- Some properties of a detergent-solubilized NADPH-cytochrome c(cytochrome P-450) reductase purified by biospecific affinity chromatography.Journal of Biological Chemistry, 1976
- SEPARATION AND PURIFICATION OF 2 FORMS OF HEPATIC CYTOCHROME-P-450 FROM UNTREATED RABBITS1976
- The Carbon Monoxide-binding Pigment of Liver MicrosomesJournal of Biological Chemistry, 1964
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951