AbstractThe binding of purine nucleotides to intact brown fat mitochondria is re-examined. In addition to the previously reported high affinity binding site, a low-affinity site is found, which requires several minutes to saturate. Only the high affinity site is functional in regulating the proton and halide permeabilities of the mitochondria. The low affinity site can introduce errors in the use of nucleotide binding to quantitate the Mr 32 000 uncoupling protein unique to these mitochondria
AbstractFatty acids activate the uncoupling protein UCP1 by a still controversial mechanism. Two mod...
AbstractFree fatty acids, natural uncouplers of oxidative phosphorylation, are shown to differ from ...
The aim of the present study was to investigate the biosynthesis of the ATP synthase in various tiss...
AbstractThe binding of purine nucleotides to intact brown fat mitochondria is re-examined. In additi...
AbstractTetranitromethane reacts with the uncoupling protein of intact brown fat mitochondria. The c...
AbstractA concerted function of purine nucleotide (PN) binding and fatty acid (FA) release from the ...
AbstractLoose coupling of thermogenic mitochondira of brown adipose tissue is related to a high prot...
AbstractATP derivatives spin-labeled (SL) at C8, N6, C2′ or C3′ were employed in binding studies wit...
Proton leak pathways uncouple substrate oxidation from ATP synthesis in mitochondria. These pathways...
AbstractThe activity of uncoupling protein-1 (UCP1) is rate-limiting for nonshivering thermogenesis ...
AbstractSpecific permeability properties of the inner membrane of brown adipose tissue mitochondria ...
AbstractThe molecular mechanism responsible for the regulation of the mitochondrial membrane proton ...
SummaryModulation of cellular energy expenditure is fundamental to normal and pathological cell grow...
Uncoupling protein 1 (UCP1) catalyzes fatty acid-activated, purine nucleotide-sensitive proton leak ...
AbstractBrown fat is a thermogenic organ that allows newborns and small mammals to maintain a stable...
AbstractFatty acids activate the uncoupling protein UCP1 by a still controversial mechanism. Two mod...
AbstractFree fatty acids, natural uncouplers of oxidative phosphorylation, are shown to differ from ...
The aim of the present study was to investigate the biosynthesis of the ATP synthase in various tiss...
AbstractThe binding of purine nucleotides to intact brown fat mitochondria is re-examined. In additi...
AbstractTetranitromethane reacts with the uncoupling protein of intact brown fat mitochondria. The c...
AbstractA concerted function of purine nucleotide (PN) binding and fatty acid (FA) release from the ...
AbstractLoose coupling of thermogenic mitochondira of brown adipose tissue is related to a high prot...
AbstractATP derivatives spin-labeled (SL) at C8, N6, C2′ or C3′ were employed in binding studies wit...
Proton leak pathways uncouple substrate oxidation from ATP synthesis in mitochondria. These pathways...
AbstractThe activity of uncoupling protein-1 (UCP1) is rate-limiting for nonshivering thermogenesis ...
AbstractSpecific permeability properties of the inner membrane of brown adipose tissue mitochondria ...
AbstractThe molecular mechanism responsible for the regulation of the mitochondrial membrane proton ...
SummaryModulation of cellular energy expenditure is fundamental to normal and pathological cell grow...
Uncoupling protein 1 (UCP1) catalyzes fatty acid-activated, purine nucleotide-sensitive proton leak ...
AbstractBrown fat is a thermogenic organ that allows newborns and small mammals to maintain a stable...
AbstractFatty acids activate the uncoupling protein UCP1 by a still controversial mechanism. Two mod...
AbstractFree fatty acids, natural uncouplers of oxidative phosphorylation, are shown to differ from ...
The aim of the present study was to investigate the biosynthesis of the ATP synthase in various tiss...