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At least 541 records · Page 30Linked to original sources
PubMed1985

FAD-dependent malate dehydrogenase from Mycobacterium smegmatis: activation of the lipid-depleted enzyme by incorporation into cardiolipin liposome.

The lipid-depleted, enzymatically inactive malate dehydrogenase isolated from Mycobacterium smegmatis membrane was found to be incorporated spontaneously into cardiolipin liposome, but not into phosphatidylcholine liposome, as was revealed by electron spin resonance spectra with the use of 5-doxylstearic acid as a spin probe in the phospholipid liposomes. In addition, sucrose density gradient centrifugation in 0.5 M KCl showed hydrophobic interaction of the enzyme with cardiolipin liposome and further proved that the enzyme thus interacted hydrophobically with cardiolipin liposome became enzymatically active. From the results obtained above, it was concluded that the lipid-depleted, enzymatically inactive malate dehydrogenase isolated from M. smegmatis membrane was found to be activated by incorporating into the hydrophobic region of cardiolipin liposome.

Cardiolipins↗
PubMed1988

Effect of styrene and other alkyl benzene derivatives on oxidation of FAD- and NAD-linked substrates in rat liver mitochondria.

The effect on energetic metabolism of rat liver mitochondria (RLM) of styrene and other aliphatic benzene derivatives, i.e. toluene, ethylbenzene, alpha-methylstyrene and butylbenzene, is studied. It is shown that these compounds uncouple oxidative phosphorylation and this effect is connected with the stimulation of passive entry of protons into mitochondria. The relationship between hydrophobicity of these compounds and their biological activity and mechanism of uncoupling effect are discussed.

Adenosine Triphosphatases↗