PROTEIN AS THE MITOCHONDRIAL SITE FOR ACTION OF UNCOUPLING PHENOLS.
Phenolic reagents which uncouple oxidative phosphorylation are bound to the protein moiety of mitochondria. This interaction may induce configurational changes in the enzymes of oxidative phosphorylation, and these changes could be responsible for the uncoupling phenomenon
D000818:Animals; D000963:Antimetabolites; D002417:Cattle; D002845:Chromatography; D004140:Dinitrophenols; D007202:Indicators and Reagents; D008099:Liver / Q000166:cytology*; D008660:Metabolism; D008928:Mitochondria; D010085:Oxidative Phosphorylation; D010600:Pharmacology; D010636:Phenols; D011506:Proteins; D051381:Rats; D012106:Research; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D013053:Spectrophotometry
D000963:Antimetabolites; D004140:Dinitrophenols; D007202:Indicators and Reagents; D010636:Phenols; D011506:Proteins; D012709:Serum Albumin; D012710:Serum Albumin, Bovine
ANTIMETABOLITES; CHROMATOGRAPHY; DINITROPHENOLS; EXPERIMENTAL LAB STUDY; LIVER CYTOLOGY; METABOLISM; MITOCHONDRIA; OXIDATIVE PHOSPHORYLATION; PHARMACOLOGY; PHENOLS; PROTEINS; RATS; SERUM ALBUMIN, BOVINE; SPECTROPHOTOMETRY