Zobrazeno 1 - 6
of 6
pro vyhledávání: '"R N, Ishmukhamedov"'
Publikováno v:
Biokhimiia (Moscow, Russia). 59(2)
The pore with an effective diameter of 6.0 A is a Ca(2+)-channel of the inner mitochondrial membrane. Transport of nonelectrolytes through the pore is inhibited by ruthenium red, a specific Ca2+ transport inhibitor, and by polyanions which bind to th
Autor:
M Kh, Gaĭnutdinov, V V, Konov, R N, Ishmukhamedov, T N, Zakharova, M A, Khalilova, M I, Asparov
Publikováno v:
Biokhimiia (Moscow, Russia). 58(5)
Small concentrations of low molecular weight modulators of the functional state of rat liver cytoplasm mitochondria, which uncouple oxidative phosphorylation, induce phosphate-dependent transport of potassium and hydrogen ions. In contrast, high conc
Autor:
M Kh, Gaĭnutdinov, V V, Konov, R N, Ishmukhamedov, T N, Zakharova, M A, Khalilova, K S, Safarov
Publikováno v:
Biokhimiia (Moscow, Russia). 57(11)
Studies of swelling of rat liver mitochondria in isoosmotic solutions of nonelectrolytes in the presence of respiration inhibitors revealed that submicromolar concentrations of Ca2+ increase the diameter of pores in the inner mitochondrial membrane--
Autor:
M Kh, Gaĭnutdinov, V V, Konov, R N, Ishmukhamedov, T N, Zakharova, M A, Khalilova, Z A, Mamatova, M I, Asrarov, S I, Mirmakhmudova
Publikováno v:
Biokhimiia (Moscow, Russia). 55(12)
In vivo thyroid hormones control the binding to mitochondria of low molecular weight water-soluble cytoplasmic mediators that are capable to induce oxidative phosphorylation uncoupling, by increasing the sensitivity of mitochondria to the effects of
Publikováno v:
Biokhimiia (Moscow, Russia). 55(7)
A water-soluble thermostable factor from rat liver cytoplasm whose activity decreases during starvation, causes the uncoupling of oxidative phosphorylation and stimulates pyruvate oxidation in rat liver mitochondria. The activity of this factor is in
Publikováno v:
Biokhimiia (Moscow, Russia). 53(2)
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 phosp