Determination of Drug−Plasma Protein Binding Kinetics and Equilibria by Chromatographic Profiling:  Exemplification of the Method Usingl-Tryptophan and Albumin

2002 ◽  
Vol 74 (2) ◽  
pp. 446-452 ◽  
Author(s):  
Ann M. Talbert ◽  
George E. Tranter ◽  
Elaine Holmes ◽  
Peter L. Francis
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Binding Kinetics ◽  
Drug Plasma ◽  
Protein Binding Kinetics ◽  
Chromatographic Profiling

Determination of drug plasma protein binding by solid phase microextraction

2006 ◽  
Vol 95 (8) ◽  
pp. 1712-1722 ◽  
Author(s):  
Florin Marcel Musteata ◽  
Janusz Pawliszyn ◽  
Mark G. Qian ◽  
Jing-Tao Wu ◽  
Gerald T. Miwa
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Solid Phase Microextraction ◽  
Solid Phase ◽  
Drug Plasma

Plasma protein binding kinetics of valproic acid over a broad dosage range: therapeutic implications

1993 ◽  
Vol 18 (3) ◽  
pp. 191-197 ◽  
Author(s):  
M. J. Gómez Bellver ◽  
M. J. Garcéa Sánchez ◽  
A. C. Alonso Gonzalez ◽  
D. Santos Buelga ◽  
A. Dominguez–Gil
Keyword(s):  
Valproic Acid ◽  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Binding Kinetics ◽  
Dosage Range ◽  
Therapeutic Implications ◽  
Protein Binding Kinetics ◽  
Kinetics Of

Plasma protein binding and endothelial enzyme interactions in the lung

1989 ◽  
Vol 66 (6) ◽  
pp. 2617-2628 ◽  
Author(s):  
J. H. Linehan ◽  
C. A. Dawson ◽  
R. D. Bongard ◽  
T. A. Bronikowski ◽  
D. L. Roerig
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Dissociation Rate ◽  
Binding Kinetics ◽  
Dilution Method ◽  
Bolus Transit ◽  
Protein Binding Kinetics ◽  
Transient Plasma ◽  
Kinetics Of

The influence of plasma albumin binding of the synthetic angiotensin-converting enzyme (ACE) substrate [3H]benzoyl-phenylalanyl-alanyl-proline (BPAP) on BPAP hydrolysis by pulmonary endothelial ACE was studied in isolated rabbit lungs perfused with a salt solution containing either 5% bovine serum albumin (BSA) or 5% dextran. The single-pass indicator-dilution method was used to measure the fraction (M) of [3H]BPAP hydrolyzed. Lung M was greater with albumin-free perfusate than when BSA was present. M decreased as the time (ti) that the BPAP was in contact with the BSA before reaching the lung was increased, suggesting that some BSA binding sites for BPAP were not in equilibrium during bolus transit through the lungs. The M vs. ti data were correlated using a model incorporating both rapid and slow binding kinetics of BPAP and BSA. For the slow BPAP-BSA interaction, the dissociation rate constant was approximately 0.015 s-1, and the fraction of the BPAP bound to these slowly equilibrating sites at equilibrium was approximately 22%. The results indicate that transient plasma protein binding kinetics can affect lung BPAP hydrolysis.

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