| Autor: |
Oester, Y.T., Keresztes‐Nagy, Steven, Mais, Roland F., Becktel, Jack, Zaroslinski, John F. |
| Zdroj: |
Journal of Pharmaceutical Sciences; November 1976, Vol. 65 Issue: 11 p1673-1677, 5p |
| Abstrakt: |
The in vitrobinding of warfarin by human serum albumin was studied at various temperatures and at pH 7.4 by a frontal gel filtration technique. The results can be best described in terms of a two class‐of‐binding site model, in which the numbers of primary and secondary sites are constrained to the average values for all experiments (n1= 1.38 and n2= 3.73). Analysis of the temperature dependence of the binding yielded the following thermodynamic parameters: ΔH1= –2.55 kcal/mole, αS1= 16.1 eu, and ΔF1= –7.34 kcal/mole for the primary binding and ΔH2= –5.08 kcal/mole, ΔS2= –1.10 eu, and ΔF2= 4.72 kcal/mole for the secondary binding. Calculations based on these results showed that, for the therapeutic concentration range, warfarin was over 99% bound to albumin present in physiological concentration. These findings are compared and contrasted to binding data in the literature for warfarin and salicylate. |
| Databáze: |
Supplemental Index |
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