Effect of free fatty acid anion on the in vitro binding of 1-anilino-8-naphthalene sulfonate to cytoplasmic proteins from rat liver.
The influence of oleate ion, a free fatty acid anion, on the binding characteristics of 1-anilino-8-naphthalene sulfonate (ANS) with the cytoplasmic proteins (Y and Z) from rat liver has been examined using fluorescence spectroscopy. ANS binds strongly with both ligandin (Y) and Z protein at a single binding site with dissociation constants of 0.6 and 1.4 micron respectively. Increasing concentrations of oleate ion decreased the ANS binding with either protein by competing with the ANS binding site. Relative binding constant of oleate ion for the hepatic ligandin or Z protein was about 2 micron as determined from the competitive inhibition of ANS binding. These results suggest that variations in the hepatic cytoplasmic free fatty acid concentration may be important in regulating the capacity of Y and Z proteins to transport other organic anions.
D000817:Anilino Naphthalenesulfonates / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D003593:Cytoplasm / Q000187:drug effects / Q000378:metabolism; D005230:Fatty Acids, Nonesterified / Q000494:pharmacology*; D066298:In Vitro Techniques; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D008297:Male; D009829:Oleic Acids / Q000494:pharmacology; D011485:Protein Binding / Q000187:drug effects; D011487:Protein Conformation; D051381:Rats; D013050:Spectrometry, Fluorescence
D000817:Anilino Naphthalenesulfonates; D005230:Fatty Acids, Nonesterified; D009829:Oleic Acids