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Inner mitochondrial membranes bound to concanavalin A–sepharose display succinate dehydrogenase, ATPase, and cytochrome oxidase activity
Author(s) -
Strasser Reto J.,
Millán Lourdes,
Darszon Alberto
Publication year - 1992
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260391103
Subject(s) - submitochondrial particle , concanavalin a , membrane , f atpase , sepharose , cytochrome c oxidase , biochemistry , succinate dehydrogenase , oligomycin , chemistry , cytochrome , oxidase test , enzyme , atpase , chromatography , thylakoid , chloroplast , in vitro , gene
A fraction (15–20% of the total protein) of a preparation of bovine submitochondrial particles (SMPs) binds to concanavalin A–sepharose. The bound membranes displayed succinate dehydrogenase, cytochrome oxidase, and ATPase activity, which, as in SMPs, were inhibited by malonate, cyanide, and oligomycin, respectively. These results indicate that the bound membranes are inner mitochondrial membranes and that they contain a glycoprotein which was recognized by concanavalin A. It was possible to repeatedly perform the three enzyme assays, one after the other, in the same gel with the bound membranes. Long‐term stability tests (22 days) showed that cytochrome oxidase was much more stable in the membranes bound to the gel than in SMPs, while the ATPase activity decayed at a similar rate in the two conditions. Thus, inner mitochondrial membranes bound to ConA–Sepharose appear to be a potentially interesting model for the study of immobilized multienzymatic complexes.