Displacement of sulphobromophthalein from albumin and fatty-acid-binding protein by oleic acid.
The absorption of sulphobromophthalein changes upon addition of bovine serum albumin or fatty-acid-binding protein at pH 8.4. The sulphobromophthalein spectrum is changed most drastically after the addition of albumin than in the presence of fatty-acid-binding protein isolated from rat liver, suggesting as a first approximation that binding capacity of albumin is much higher than that of fatty-acid-binding protein. When both soluble proteins are saturated with oleic acid it is observed a decrease in the binding of sulphobromophthalein which suggests that the presence of fatty acids in those soluble proteins may affect the binding of other ligands.
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D000818:Animals; D001667:Binding, Competitive / Q000187:drug effects; D002352:Carrier Proteins / Q000378:metabolism*; D002417:Cattle; D002850:Chromatography, Gel; D003956:Dialysis; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D019301:Oleic Acid; D009829:Oleic Acids / Q000494:pharmacology*; D011485:Protein Binding / Q000187:drug effects; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013053:Spectrophotometry; D013448:Sulfobromophthalein / Q000097:blood*
D002352:Carrier Proteins; C490174:Fabp7 protein, rat; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D009829:Oleic Acids; D013448:Sulfobromophthalein; D012710:Serum Albumin, Bovine; D019301:Oleic Acid