|
pubmed:abstractText |
The binding of bile salts to proteins in rat plasma and rat lymph has been investigated. Under the non-equilibrium conditions of gel chromatography no binding of glycochenodeoxycholate or glycocholate to any of the lymph proteins was observed. In contrast, plasma bound a proportion of both bile salts. When lymph was treated with charcoal, binding of glycochenodeoxycholate to a protein with a molecular weight identical to albumin occurred. Equilibrium binding studies showed that the binding of glycocholate to partially purified plasma albumin exhibited saturation kinetics with a dissociation constant of 2 x 10(-4) M. In contrast, the binding of glycocholate to lymph albumin was non-saturable. Potassium oleate, when added to plasma in a free fatty acid : albumin molar ratio of 3.8 : 1, almost completely inhibited the binding of chenodeoxycholate to plasma albumin. The endogenous free fatty acid : albumin ratios found in systemic plasma and lymph were 0.6 : 1 and 9.2 : 1, respectively. It is suggested that the high free fatty acid concentrations found in lymph inhibit the binding of bile salts to albumin.
|
