Posttranslational and direct integration of heme oxygenase into microsomes.
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.
Yoshida
T
T
Department of Molecular and Pathological Biochemistry, Yamagata University School of Medicine, Japan.
Sato
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M
D000818:Animals; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D006419:Heme Oxygenase (Decyclizing) / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D051381:Rats; D011919:Rats, Inbred Strains; D014357:Trypsin / Q000378:metabolism
D006899:Mixed Function Oxygenases; D006419:Heme Oxygenase (Decyclizing); D014357:Trypsin