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Equilibrium between monomeric and dimeric mitochondrial F1–inhibitor protein complexes
Author(s) -
Domı́nguez-Ramı́rez L.,
Mendoza-Hernandez G.,
Carabez-Trejo A.,
Gómez-Puyou A.,
Tuena de Gómez-Puyou M.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02979-9
Subject(s) - monomer , dimer , chemistry , inhibitor protein , size exclusion chromatography , solubilization , mitochondrion , electron microscope , chromatography , biochemistry , organic chemistry , enzyme , polymer , physics , optics
Mg‐ATP particles from bovine heart mitochondria have more than 95% of their F1 in complex with the inhibitor protein (IF1). The F1–IF1 complex was solubilized and purified. The question addressed was if this naturally occurring complex existed as monomers or dimers. Size exclusion chromatography and electron microscopy showed that most of the purified F1–IF1 complex was a dimer of two F1–IF1. As determined by the former method, the relative concentrations of dimeric and monomeric F1–IF1 depended on the concentration of protein that was applied to the column. Apparently, there is an equilibrium between the two forms of F1–IF1.