Effect of experimental hypoalbuminemia on the plasma protein binding of tolmetin
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The purpose of this work was to study tolmetin plasma protein binding in an experimental model of hypoalbuminemia in the rat. Hypoalbuminemia was produced by repetitive plasmapheresis, achieving a 26.2 ± 4.6%25 reduction in albumin circulating levels. Rats then received a 100 mg/kg oral tolmetin dose. Control rats received oral tolmetin 10, 56 or 100 mg/kg. Tolmetin plasma protein binding was determined by an ultrafiltration technique using an in vivo pharmacokinetic approach. Plasma protein binding data for the 3 doses studies in control animals could be described considering a single binding site with Kd = 21.9 ± 2.1 μM and N = 0.98 ± 0.05 sites per molecule of albumin. For hypoalbuminemic rats Kd was significantly increased (p < 0.05), while there was no significant change in the number of binding site per albumin molecule (Kd = 131.6 ± 38.1 μM and N = 1.58 ± 0.77). Our results show that hypoalbuminemia produces a disproportionate increase in the free fraction of tolmetin, not only by reducing albumin concentration, but also by a decrease in affinity. The mechanism responsible of such changes in affinity remains to be elucidated. © 2002 Elsevier Science Inc. All rights reserved.
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Experimental hypoalbuminemia; Protein-binding; Tolmetin albumin; tolmetin; animal experiment; animal model; article; binding site; controlled study; dose response; drug blood level; drug protein binding; hypoalbuminemia; male; nonhuman; plasmapheresis; protein blood level; rat; ultrafiltration; Animals; Protein Binding; Rats; Rats, Wistar; Serum Albumin; Tolmetin; Animalia
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