Cytochrome P-450 isozyme LM3b from rabbit liver microsomes. Induction by triacetyloleandomycin purification and characterization.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference39 articles.
1. Induction by Triacetyloleandomycin and partial purification of a LM3 form of cytochrome P-450 from rabbit liver microsomes
2. Self-induction by triacetyloleandomycin of its own transformation into a metabolite forming a stable 456 nm-absorbing complex with cytochrome P-450
3. Properties of electrophoretically homogeneous constitutive forms of liver microsomal cytochrome P-450.
4. Proceedings of the 4th International Conference on Cytochrome P-450: Biochemistry, Biophysics and Environmental Implications;Bonfils,1982
5. Purified liver microsomal cytochrome P-450. Separation and characterization of multiple forms.
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2. Cytochrome P450 in rat astrocytes in vivo and in vitro: Intracellular localization and induction by phenytoin;Journal of Neuroscience Research;1994-12-01
3. Human liver microsomal cytochrome P450 3A isozymes mediated vindesine biotransformation;Biochemical Pharmacology;1993-02
4. [55] Cytochrome P450 metabolic intermediate complexes from macrolide antibiotics and related compounds;Methods in Enzymology;1991
5. Purification of a sheep liver cytochrome P-450 from the P450IIIA gene subfamily;Biochemical Pharmacology;1990-03
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