title: PROTEIN AS THE MITOCHONDRIAL SITE FOR ACTION OF UNCOUPLING PHENOLS.
abstract: 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
mesh_terms: 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
chemical_list: D000963:Antimetabolites; D004140:Dinitrophenols; D007202:Indicators and Reagents; D010636:Phenols; D011506:Proteins; D012709:Serum Albumin; D012710:Serum Albumin, Bovine
keywords: ANTIMETABOLITES; CHROMATOGRAPHY; DINITROPHENOLS; EXPERIMENTAL LAB STUDY; LIVER CYTOLOGY; METABOLISM; MITOCHONDRIA; OXIDATIVE PHOSPHORYLATION; PHARMACOLOGY; PHENOLS; PROTEINS; RATS; SERUM ALBUMIN, BOVINE; SPECTROPHOTOMETRY