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PMID: 3028387 Published · ppublish English Journal Article

Localization of enzyme for heme attachment to apocytochrome c in yeast mitochondria.

Biochemical and biophysical research communications ·Vol. 141 ·No. 3 ·1986-12-30 ·Pages 1145-50

Enosawa S, Ohashi A

Abstract

Fractionation of yeast mitochondria by controlled hypotonic treatment revealed that the enzyme for heme attachment to apocytochrome c was localized in mitochondrial inner membrane. Trypsin digestion of mitoplasts resulted in a considerable loss of enzymatic activity, whereas the enzyme in intact mitochondria resisted the digestion. Triton X-100 solubilized the enzyme from the membrane but high concentration of salt did not. These results reveal that the enzyme for heme attachment is localized in mitochondrial inner membrane facing the cytoplasmic surface.

MeSH Terms
Apoproteins/metabolism Cell Fractionation Cytochrome c Group/metabolism Cytochromes c Heme/metabolism Intracellular Membranes/enzymology Lyases Mitochondria/enzymology Octoxynol Polyethylene Glycols Saccharomyces cerevisiae/enzymology Solubility Transferases/metabolism Trypsin/metabolism
Chemicals
Apoproteins Cytochrome c Group Polyethylene Glycols Heme Octoxynol Cytochromes c Transferases Trypsin Lyases cytochrome C synthetase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Enosawa S
Ohashi A
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1986-12-30
Pages
1145-50
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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