Non-equilibrium binding of spermine to mitochondrial membranes is studied in rat liver mitochondria by applying a new thermodynamic treatment of ligand-receptor interactions (Di Note, V., Dalla Via, L., Toninello, A. and Vidali, M. (1996) Macromol. Theory Simul. 5, 165-181). The presence on mitochondrial membranes of two spermine binding sites, both with monocoordination, is demonstrated. The calculated binding energy is characteristic for weak interactions. The treatment allows also to evaluate the variations of the molar fraction ratio of spermine bound to sites 1 and 2 as function of total bound spermine. The possible role of the two sites is discussed
Further study of the mitochondrial transport of spermine (Toninello et al. (1988) J. Biol. Chem. 263...
Spermine penetrates the mitochondrial matrix at significant rates which increase sharply and non-ohm...
Spermine is taken up by mammalian mitochondria and this process needs to identify its catabolic path...
AbstractNon-equilibrium binding of spermine to mitochondria) membranes is studied in rat liver mitoc...
The binding of spermidine and putrescine to mitochondrial membranes was studied by applying a thermo...
Thermodynamic analysis of spermine binding to mitochondria treated with ruthenium red and deenergize...
Free energy changes during spermine binding to rat liver mitochondria have been determined by m...
This study evaluated the effect of the anticancer drug methylglyoxal-bis( guanylhydrazone) (MGBG) on...
In the present study, the voltage-dependent mechanism of spermine transport in liver mitochondria [T...
Mg(2+) competitively inhibits spermine transport in energized rat liver mitochondria (RLM) and exhib...
The results indicated here, together with those previously reported, show that spermine, ubiquitous ...
This investigation is aimed at defining the structural requirements for aliphatic polyamines...
This paper reports a detailed analysis on the time dependence of affinity constants. These studies w...
At concentrations of 0.5-1.0 mM, spermine fully prevents the fall of membrane potential induced in r...
AbstractThermodynamic analysis of spermine binding to mitochondria treated with ruthenium red and de...
Further study of the mitochondrial transport of spermine (Toninello et al. (1988) J. Biol. Chem. 263...
Spermine penetrates the mitochondrial matrix at significant rates which increase sharply and non-ohm...
Spermine is taken up by mammalian mitochondria and this process needs to identify its catabolic path...
AbstractNon-equilibrium binding of spermine to mitochondria) membranes is studied in rat liver mitoc...
The binding of spermidine and putrescine to mitochondrial membranes was studied by applying a thermo...
Thermodynamic analysis of spermine binding to mitochondria treated with ruthenium red and deenergize...
Free energy changes during spermine binding to rat liver mitochondria have been determined by m...
This study evaluated the effect of the anticancer drug methylglyoxal-bis( guanylhydrazone) (MGBG) on...
In the present study, the voltage-dependent mechanism of spermine transport in liver mitochondria [T...
Mg(2+) competitively inhibits spermine transport in energized rat liver mitochondria (RLM) and exhib...
The results indicated here, together with those previously reported, show that spermine, ubiquitous ...
This investigation is aimed at defining the structural requirements for aliphatic polyamines...
This paper reports a detailed analysis on the time dependence of affinity constants. These studies w...
At concentrations of 0.5-1.0 mM, spermine fully prevents the fall of membrane potential induced in r...
AbstractThermodynamic analysis of spermine binding to mitochondria treated with ruthenium red and de...
Further study of the mitochondrial transport of spermine (Toninello et al. (1988) J. Biol. Chem. 263...
Spermine penetrates the mitochondrial matrix at significant rates which increase sharply and non-ohm...
Spermine is taken up by mammalian mitochondria and this process needs to identify its catabolic path...