NDLI: Hepatic Mitochondrial Cytochrome P-450 System

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Hepatic Mitochondrial Cytochrome P-450 System

Content Provider	Semantic Scholar
Author	Banavadi Niranjan S. Q. Haider Raza S. Rass M. Shayiq S. Colin Jefcoatev Narayan Avadhani S.
Copyright Year	2001
Abstract	Hepatic mitoplasts from 3-methylcholanthrenetreated rats contain cytochrome P-450 which can metabolize polycyclic aromatic hydrocarbons like benzo(a)pyrene. Mitochondrial cytochrome P-450 was partially purified and reconstituted in vitro using adrenodoxin and the adrenodoxin reductase electron transfer system and [‘H]benzo(a)pyrene as the substrate. A polyclonal antibody to purified microsomal P-46Oc (a major 3-methylcholanthrene-inducible form) inhibited the activity of mitochondrial enzyme in a concentration-dependent manner and also reacted with a 64-kDa protein on the immunoblots. A monoclonal antibody having exclusive specificity for P450c, on the other hand, did not inhibit the aryl hydrocarbon hydroxylase activity of the mitochondrial enzyme and showed no detectable cross-reaction with the 54-kDa mitochondrial protein. Similarly, two-dimensional analysis and immunodetection using the polyclonal antibody showed distinct molecular properties of the mitochondrial enzyme different from the similarly induced microsomal P-45Oc with respect to the isoelectric pH. In vitro translation of free polysomes from 3-methylcholanthrene-inducedliver, transport of precursor proteins by isolated mitochondria in vitro, and immunoprecipitation with the polyclonal antibody showed the presence of a 57-kDa putative precursor which is transported and processed into mature 54kDa species. These results present evidence for the true intramitochondrial location of the P-450c-antibody reactive isoform detected in 3-methylcholanthrene-induced rat liver mitochondria.
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.jbc.org/content/263/1/575.full.pdf
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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