Abstract
Binding of bilirubin to human serum albumin was studied by estimation of the free bilirubin concentration from the rate of oxidation with hydrogen peroxide and peroxidase, and by spectrophotometry: nI = 1, kI = 7 x 10(7) l/mol; nII = 1, kII = 5 x 10)5) l/mol, at pH 7.4, 37 degrees C, ionic strength 0.1. Palmitate or oleate in excess of 4 mol per mol albumin, influences the high-affinity binding of bilirubin as described by an empirical equation. Theoretical consideration of competitive displacement of a biologically active substance, firmly bound in an inactive state to a macromolecular carrier, demonstrates that significant displacement may occur on addition of another ligand with a lower binding constant. Displacement of bilirubin from its high-infinity site by fatty acids and drugs is thermodynamically feasible and probably clinically important.
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