Thermodynamic analysis of spermine binding to mitochondria treated with ruthenium red and deenergized with either FCCP or antimycin A confirms the presence of two polyamine binding sites, S-1 and S-2, both with monocoordination, as previously observed in energized mitochondria [Dalla Via et al., Biochim, Biophys. Acta 1284 (1996) 247-252], Both sites undergo a marked change in binding capacity and binding affinity upon mitochondrial deenergization. This change is most likely responsible for the incomplete or delayed spermine-mediated inhibition of the permeability transition induced in deenergized mitochondria.
Spermine binding to liver mitochondria deenergized by ruthenium red plus either FCCP or antimycin A
DALLA VIA, LISA;DI NOTO, VITO;TONINELLO, ANTONIO
1998
Abstract
Thermodynamic analysis of spermine binding to mitochondria treated with ruthenium red and deenergized with either FCCP or antimycin A confirms the presence of two polyamine binding sites, S-1 and S-2, both with monocoordination, as previously observed in energized mitochondria [Dalla Via et al., Biochim, Biophys. Acta 1284 (1996) 247-252], Both sites undergo a marked change in binding capacity and binding affinity upon mitochondrial deenergization. This change is most likely responsible for the incomplete or delayed spermine-mediated inhibition of the permeability transition induced in deenergized mitochondria.File in questo prodotto:
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