The results indicated here, together with those previously reported, show that spermine, ubiquitous polyamine, while promoting the transmembrane translocation of casein kinase II (CKII) across the outer membrane to more internal compartments of rat liver mitochondria, promotes the binding of casein kinase I (CKI) to the external surface of outer mitochondrial membrane but inhibits its spontaneously occurring binding to more internal structures. (C) 1994 Academic Press, Inc
AbstractSpermine (0.5–2 mM) promoted the translocation of phosphatidate phosphohydrolase from the so...
Protein kinase C is reported to exist in two membrane-bound states: a reversible one which can be di...
Further study of the mitochondrial transport of spermine (Toninello et al. (1988) J. Biol. Chem. 263...
Spermine, ubiquitous intracellular polyamine, is able to promote the transmembrane translocation of ...
Spermine prevents glutathione release induced in rat liver mitochondria by the combined addition of ...
At concentrations of 0.5-1.0 mM, spermine fully prevents the fall of membrane potential induced in r...
AbstractThe effect of spermine on the permeability transition of the inner mitochondrial membrane of...
Non-equilibrium binding of spermine to mitochondrial membranes is studied in rat liver mitochondria ...
International audienceThe polyamine spermine is transported into the matrix of various types of mito...
Mg(2+) competitively inhibits spermine transport in energized rat liver mitochondria (RLM) and exhib...
AbstractNon-equilibrium binding of spermine to mitochondria) membranes is studied in rat liver mitoc...
Thermodynamic analysis of spermine binding to mitochondria treated with ruthenium red and deenergize...
The in vitro mechanism by which polyamines affect protein kinase C (PK C) activation process was inv...
In the absence of exogenous Ca(2+) and Mg(2+) and in the presence of EGTA, which favours the release...
Abstract: Cytosolic spermidine/spermine acetyltransferase (SSAT) catalyzes the acetylation of the N-...
AbstractSpermine (0.5–2 mM) promoted the translocation of phosphatidate phosphohydrolase from the so...
Protein kinase C is reported to exist in two membrane-bound states: a reversible one which can be di...
Further study of the mitochondrial transport of spermine (Toninello et al. (1988) J. Biol. Chem. 263...
Spermine, ubiquitous intracellular polyamine, is able to promote the transmembrane translocation of ...
Spermine prevents glutathione release induced in rat liver mitochondria by the combined addition of ...
At concentrations of 0.5-1.0 mM, spermine fully prevents the fall of membrane potential induced in r...
AbstractThe effect of spermine on the permeability transition of the inner mitochondrial membrane of...
Non-equilibrium binding of spermine to mitochondrial membranes is studied in rat liver mitochondria ...
International audienceThe polyamine spermine is transported into the matrix of various types of mito...
Mg(2+) competitively inhibits spermine transport in energized rat liver mitochondria (RLM) and exhib...
AbstractNon-equilibrium binding of spermine to mitochondria) membranes is studied in rat liver mitoc...
Thermodynamic analysis of spermine binding to mitochondria treated with ruthenium red and deenergize...
The in vitro mechanism by which polyamines affect protein kinase C (PK C) activation process was inv...
In the absence of exogenous Ca(2+) and Mg(2+) and in the presence of EGTA, which favours the release...
Abstract: Cytosolic spermidine/spermine acetyltransferase (SSAT) catalyzes the acetylation of the N-...
AbstractSpermine (0.5–2 mM) promoted the translocation of phosphatidate phosphohydrolase from the so...
Protein kinase C is reported to exist in two membrane-bound states: a reversible one which can be di...
Further study of the mitochondrial transport of spermine (Toninello et al. (1988) J. Biol. Chem. 263...