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Purification and characterization of two unique forms of cytochrome P-450 from rabbit nasal microsomes

X X Ding1, M J Coon

  • 1Department of Biological Chemistry, Medical School, University of Michigan, Ann Arbor 48109.

Biochemistry
|November 1, 1988
PubMed

Insights

Two distinct cytochrome P-450 forms, P-450NMa and P-450NMb, were purified from rabbit nasal microsomes. These enzymes metabolize ethanol, procarcinogens, and testosterone, showing unique activity profiles and spin states.

Area of Science:

  • Biochemistry
  • Pharmacology
  • Toxicology

Background:

  • Cytochrome P-450 enzymes are crucial for metabolizing xenobiotics and endogenous compounds.
  • Nasal P-450 forms play a significant role in the metabolism of inhaled substances, including procarcinogens.
  • Understanding specific P-450 isoforms is key to predicting drug efficacy and toxicity.

Purpose of the Study:

  • To purify and characterize novel cytochrome P-450 forms from rabbit nasal microsomes.
  • To investigate the substrate specificity and catalytic activities of these purified nasal P-450 enzymes.
  • To compare the properties of these nasal P-450 forms with known hepatic P-450 enzymes.

Main Methods:

  • Purification of cytochrome P-450 to electrophoretic homogeneity from rabbit nasal microsomes.
  • Characterization using amino acid composition, absorption spectra, peptide mapping, and N-terminal sequencing.
  • Reconstitution assays with NADPH-cytochrome P-450 reductase and phospholipid to determine enzymatic activity.
  • Substrate metabolism studies using ethanol, procarcinogens (N-nitrosodiethylamine, phenacetin, hexamethylphosphoramide), and testosterone.

Main Results:

  • Two distinct cytochrome P-450 forms, P-450NMa and P-450NMb, were isolated with molecular weights of 49,500 and 51,000 Da, respectively.
  • These nasal forms exhibited unique amino acid compositions, spectral properties, and N-terminal sequences, differentiating them from each other and other known P-450s.
  • P-450NMa showed high activity in ethanol oxidation and procarcinogen metabolism, while P-450NMb displayed lower rates for these substrates.
  • Both forms metabolized testosterone differently: P-450NMa at the 17-position and P-450NMb at the 15α, 16α, and 19-positions.
  • P-450NMa was low-spin and P-450NMb was predominantly high-spin in their ferric forms.
  • These nasal P-450 forms constituted the major P-450 content in nasal microsomes but were not detected in hepatic microsomes.

Conclusions:

  • Rabbit nasal microsomes contain at least two unique cytochrome P-450 forms, P-450NMa and P-450NMb.
  • These enzymes possess distinct biochemical and catalytic properties, suggesting specialized roles in nasal xenobiotic metabolism.
  • The findings highlight the tissue-specific expression of P-450 enzymes and their potential involvement in the activation or detoxification of inhaled compounds.

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