Journal article
Identification of the membrane anchor of microsomal rat liver cytochrome P-450.
- Vergères G Laboratorium für Biochemie, Eidgenössische Technische Hochschule, Zürich, Switzerland.
- Winterhalter KH
- Richter C
- 1989-05-02
Published in:
- Biochemistry. - 1989
Animals
Cytochrome P-450 Enzyme System
Enzyme Induction
Freeze Fracturing
Lipid Bilayers
Male
Microscopy, Electron
Microsomes, Liver
Phenobarbital
Proteolipids
Rats
Rats, Inbred Strains
English
Cytochrome P450IIB1 isolated from rat liver microsomes was incorporated into phosphatidylcholine/phosphatidylethanolamine/phosphatidylserine (10:5:1 w/w) liposomes. Trypsinolysis of proteoliposomes and sequencing of the membrane-bound domains revealed that only one peptide, comprising amino acid residues 1-21, spans the membrane. Modification of the N-terminal methionine by membrane-impermeable fluorescein isothiocyanate occurred with the protein in solution but not in proteoliposomes. We conclude that in proteoliposomes cytochrome P-450 spans the membrane only with amino acid residues 1-21, the N-terminal methionine facing the lumen.
- Language
-
- English
- Open access status
- closed
- Identifiers
-
- DOI 10.1021/bi00435a005
- PMID 2751987
- Persistent URL
- https://sonar.ch/global/documents/47391
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