Abstract:
:Cytochrome c oxidase has been isolated from beef heart mitochondria and labeled with the fluorochrome eosin-5-maleimide (EMA) after pretreatment with mersalyl. On SDS-polyacrylamide gels, EMA fluorescence and absorption occurred at a single band corresponding to subunit III. Since only Cys 115 of the two cysteinyl residues of subunit III had been shown to be reactive towards water-soluble SH-reagents, it was concluded that this residue was the one labeled by EMA. The EMA/enzyme ratio was about 1. Gel filtration experiments have shown that upon treatment with dicyclohexylcarbodiimide, subunit III was loosened from the complex; this result suggests that the inhibitory effect of dicyclohexylcarbodiimide on the H+-translocation activity may be related to such a phenomenon.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Müller M,Azzi Adoi
10.1016/0014-5793(85)80664-5subject
Has Abstractpub_date
1985-05-06 00:00:00pages
110-4issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(85)80664-5journal_volume
184pub_type
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