[Regulation of oxidative phosphorylation, K+ ions transport and the volume of mitochondrial matrix by cytoplasmic glycopeptide and Ca2+ ions].

A thermostable low molecular weight glycopeptide containing syalic acids, which uncouples mitochondrial oxidative phosphorylation, has been detected, isolated and purified from rat liver cytoplasm. In the presence of the glycopeptide, oxidative phosphorylation in rat liver mitochondria is uncoupled by low physiological concentrations of Ca2+, which otherwise do not have any appreciable effect on the mitochondria. Oxidative phosphorylation uncoupling by the glycopeptide is accompanied by an increase of the mitochondrial volume.

[Electrogenic transport of bicarbonate ions through the internal mitochondrial membrane induced by cytoplasmic glycopeptide].

Cytoplasmatic glycopeptide-induced bicarbonate ion electrogenic transport through mitochondrial membrane has been studied. Glycopeptide, described earlier as a factor increasing inner mitochondrial membrane permeability for phosphate ions, has been also shown to induce bicarbonate ion electrogenic transport through inner mitochondrial membrane. HCO3- ion transport, induced by cytoplasm glycopeptide is realized by pH-dependent pore.

[Effect of total ischemia and 3',5'-cAMP on the activity of the thermostable cytoplasmic inhibitor of Ca2+ ion transport in rat heart mitochondria].

Activity of cytoplasmic inhibitor of Ca2+ transport in rat heart mitochondria was studied after total ischemia and incubation of heart homogenates with cAMP. Distinct inactivation of the inhibitor occurred under these conditions. The decrease of the inhibitor activity in ischemic myocardium appears to serve as a compensatory mechanism: 1.