The microsomal monooxygenase system is characterized by its broad substrate specificity which includes endogenous substrates as well as lipophilic drugs and chemicals. From in vitro investigations it was known that the relative reactivities and the pattern of products varied greatly with species, se
Chromatographic and catalytic properties of multiple forms of rabbit pulmonary cytochromes P-450
โ Scribed by Ueng, Tzuu-Huei ;Peiperl, Martha D. ;Alvares, Alvito P.
- Book ID
- 102874563
- Publisher
- John Wiley and Sons
- Year
- 1988
- Tongue
- English
- Weight
- 529 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0887-2082
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โฆ Synopsis
Rabbit pulmonary cytochrome P-450 forms 2, 5, and 6 were resolved using anion-exchange high-performance liquid chromatography (HPLC) and their properties compared with rabbit liver cytochrome P-450 isozymes LM2 and LM6. Although rabbit pulmonary form 2 and liver LM2 had similar electrophoretic mobilities and similar substrate specificities in reconstitution experiments, they differed in their HPLC elution profiles. High-performance liquid chromatography of pulmonary microsomes from rabbits treated with 3-methylcholanthrene (3-MC) revealed the induction of form 6 isozyme, which had a retention time, electrophoretic mobility, and substrate specificity similar to those of rabbit liver LM6. In reconstitution experiments, forms 2 and 6 showed the highest substrate specificities toward benzphetamine and 7-ethoxyresorufin, respectively. Rabbit lung cytochrome P-450 form 5 was relatively inactive toward all substrates tested.
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