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PMID: 2783112 Published · ppublish English Journal Article

Posttranslational and direct integration of heme oxygenase into microsomes.

Biochemical and biophysical research communications ·Vol. 163 ·No. 2 ·1989-09-15 ·Pages 1086-92

Yoshida T, Sato M

Abstract

Rat liver heme oxygenase has a large cytoplasmically exposed domain containing the N-terminus that can be cleaved from the membranes by a low concentration of trypsin, indicating that heme oxygenase is embedded in membranes with an insertion sequence near its C-terminal portion. Heme oxygenase synthesized in a cell-free system or purified from microsomes after detergent-solubilization was integrated into microsomal membranes posttranslationally and directly, like cytochrome b5.

MeSH Terms
Animals Blotting, Western Electrophoresis, Polyacrylamide Gel Heme Oxygenase (Decyclizing)/metabolism Male Microsomes, Liver/enzymology Mitochondria, Liver/metabolism Mixed Function Oxygenases/metabolism Protein Processing, Post-Translational Rats Rats, Inbred Strains Trypsin/metabolism
Chemicals
Mixed Function Oxygenases Heme Oxygenase (Decyclizing) Trypsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Yoshida T
Department of Molecular and Pathological Biochemistry, Yamagata University School of Medicine, Japan.
Sato M
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1989-09-15
Pages
1086-92
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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