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Membrane topology of microsomal cytochrome P-450: Saturation transfer EPR and freeze-fracture electron microscopy studies
- Source :
- Biochemical and Biophysical Research Communications. 171:175-181
- Publication Year :
- 1990
- Publisher :
- Elsevier BV, 1990.
-
Abstract
- The rotation of cytochrome P-450 LM2 (CYPIIB4) incorporated into large microsomal-like lipid vesicles was investigated by saturation transfer EPR using 15N- and 2H-substituted spin labels. In combination with rotational diffusion, the distribution and size of protein particles in the bilayer were studied by freeze-fracture electron microscopy. The data from both methods suggest an oligomeric and membrane-spanning aggregate for the topology of microsomal cytochrome P-450.
- Subjects :
- Cytochrome
Biophysics
Analytical chemistry
In Vitro Techniques
Biochemistry
law.invention
Diffusion
Motion
Cytochrome P-450 Enzyme System
law
Microsomes
Freeze Fracturing
Electron paramagnetic resonance
Molecular Biology
biology
Chemistry
Bilayer
Electron Spin Resonance Spectroscopy
Rotational diffusion
Cytochrome P450
Cell Biology
Microscopy, Electron
Membrane protein
Membrane topology
biology.protein
Electron microscope
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 171
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....b8bba7ac399e38c0e15debc063fe0fdb
- Full Text :
- https://doi.org/10.1016/0006-291x(90)91373-z