Membrane topology of N-terminal residues of cytochromes P-450 2B4 and 1A2

Biochem Mol Biol Int. 1994 Aug;34(1):183-90.

Abstract

The paper describes the reactivity of fluorescein isothiocyanate towards the N-terminus of cytochromes P450 2B4 and 1A2 in solution, in the natural membrane of microsomes and in proteoliposomes (cholate and ultrasonic). The results obtained indicate, that the N-terminus of microsomal or proteoliposomal cytochromes P-450 2B4 and 1A2 spans the membrane only once and faces the vesicles interior. It was suggested that of major importance in orientation of N-terminal residues in the membrane is not the hydrophobic segment itself but rather the positively charged fragment, following it.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aryl Hydrocarbon Hydroxylases*
  • Cytochrome P-450 CYP1A2
  • Cytochrome P-450 Enzyme System / chemistry
  • Cytochrome P-450 Enzyme System / isolation & purification
  • Cytochrome P-450 Enzyme System / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Fluorescein-5-isothiocyanate / chemistry*
  • Microsomes / drug effects
  • Microsomes / enzymology*
  • Microsomes / ultrastructure
  • Molecular Sequence Data
  • Octoxynol / pharmacology
  • Oxidoreductases / chemistry
  • Oxidoreductases / isolation & purification
  • Oxidoreductases / metabolism*
  • Proteolipids / metabolism
  • Rabbits
  • Spectrometry, Fluorescence
  • Steroid Hydroxylases / chemistry
  • Steroid Hydroxylases / isolation & purification
  • Steroid Hydroxylases / metabolism*

Substances

  • Proteolipids
  • proteoliposomes
  • Octoxynol
  • Cytochrome P-450 Enzyme System
  • Oxidoreductases
  • Steroid Hydroxylases
  • Aryl Hydrocarbon Hydroxylases
  • Cytochrome P-450 CYP1A2
  • steroid 15-alpha-hydroxylase
  • Fluorescein-5-isothiocyanate