Effect of sodium chlorophenoxyisobutyrate on the binding of vitamin K antagonists to human albumin in vitro

Tillement, J P; Mattei, C; Zini, Roland

doi:10.1007/bf01926292

Cited by 9 publications

(2 citation statements)

References 11 publications

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“…The effects of sodium 2-(4-chlorophenoxy)-2-methylpropanoate, the active form of clofibrate, on the possible displacement of phenindione derivatives from human albumin were investigated (41). This work was undertaken because clofibrate presumably had the same binding site on albumin as phenylbutazone.…”

Section: Physical Significance Of Protein Bindingmentioning

confidence: 99%

Binding of Drugs by Albumin Plasma Protein

Vallner

1977

Journal of Pharmaceutical Sciences

325

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Section: Physical Significance Of Protein Bindingmentioning

confidence: 99%

Binding of Drugs by Albumin Plasma Protein

Vallner

1977

Journal of Pharmaceutical Sciences

325

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“…The binding of phenylindanediones to plasma proteins was shown by Tillement (1,2), who demonstrated that the sites which bind the coumarine anticoagulants and the phenylindanedione anticoagulants are distinct. Although, the binding parameters of the coumarine anticoagulants to human serum albumin are fairly well known (3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19), little is known about those of the phenylindanediones.…”

Section: Introductionmentioning

confidence: 99%

Interactions of some phenylindanedione anticoagulants with human serum albumin

Paubel

Nivière

Payard³

et al. 1981

European Journal of Drug Metabolism and Pharmacokinetics

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This study enabled us, to define the quantitative parameters of the interactions which give rise to the formation of complexes between five phenylindanediones and albumin or polymethacryate. The existence of three attachment sites were demonstrated, by which these ligands are bound to the macromolecule. The results from the thermodynamic study of this phenomenon, together with the information supplied by; various spectroscopic methods; the formation of a complex between a synthetic polymer carrying amine functions, and the study of ligands in the presence of surfactant, were all in agreement. Furthermore, a significant correlation between the association constant and physiochemical parameters lipophilic character and acidity was obtained, leading to the conclusion that; the interactions permitting the formation of the complexes between albumin and the five anionic ligands seem to be principally hydrophobic and, to a lesser degree, electrostatic. The latter only occurred in a particular medium at sites which were mainly hydrophobic.

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Anticoagulant effect and plasma kinetics of fluorophenindione after a single dose in man

Tillement

Thebault

Mattei

et al. 1975

Eur J Clin Pharmacol

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After administration of a single loading dose (80 mg p.o.) of fluorophenindione, the prothrombin level decreased to 37% in 24 h, and the effect lasted for 48 h. Accordingly, fluorophenindione can be classified as an anticoagulant with an ""intermediate'' effect. Its elimination half-life was 31 h, which is longer than that of phenindione, because of the greater stability of the fluorinated derivate.

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Effect of sodium chlorophenoxyisobutyrate on the binding of vitamin K antagonists to human albumin in vitro

Cited by 9 publications

References 11 publications

Binding of Drugs by Albumin Plasma Protein

Binding of Drugs by Albumin Plasma Protein

Interactions of some phenylindanedione anticoagulants with human serum albumin

Anticoagulant effect and plasma kinetics of fluorophenindione after a single dose in man

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