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Title: Photoaffinity labelling of the mitochondrial uncoupling protein by [3H]azido fatty acid affects the anion channel. Author: Růzicka M, Borecký J, Hanus J, Jezek P. Journal: FEBS Lett; 1996 Mar 18; 382(3):239-43. PubMed ID: 8605977. Abstract: Brown adipose tissue (BAT) mitochondria were incubated with the azido derivative of fatty acid (hexadecanoic) containing four tritium atoms, [3H]AzHA, and among all mitochondrial proteins only a few proteins were photolabelled after irradiation with UV. It suggests the existence of specific fatty acid binding sites on mitochondrial proteins. It was also possible to label with [3H]AzHA the isolated uncoupling protein (UcP) of BAT mitochondria with a low stoichiometry--lower than one AzHA per dimeric UcP. These results together with the observed competition (i.e. prevention of photolabelling) of various UcP anionic substrates with [3H]AzHA and its dodecanoic acid analogue, suggest the existence of the specific fatty acid binding site on UcP identical with the anion channel or anion translocating site.[Abstract] [Full Text] [Related] [New Search]