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Plasma protein binding of carbamazepine

Clinical Pharmacology & Therapeutics, 1975
The binding of carbamazepine to the pro teins of human plasma has been studied using ultrafiltration techniques. In vitro studies at 37° C showed the relation between concentration of unbound drug and total drug to be linear thraugh the range of total concentration of 5 to 50 µg/ml.
Hooper W.D.   +6 more
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Plasma protein binding of norethisterone

Contraception, 1982
Norethisterone (NET) is transported in the blood stream bound to plasma proteins. It is generally believed that only the part of the hormone that is not bound to plasma proteins can exert biological activity. NET binds to albumin and, like other 19-nortestosterone derived progestins, it also binds to sex hormone binding globulin (SHBG).
V, Odlind, A, Victor, E D, Johansson
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Plasma protein binding of phencyclidine

Clinical Pharmacology and Therapeutics, 1982
In healthy male subjects (n = 12) phencyclidine (PCP) free fraction was 22.0 +/- 2.8 % (mean +/- SD). In male patients with mild to moderate alcoholic liver disease (n = 16) free fraction (23.0 +/- 3.4%) was of the same order as in healthy subjects although age and the concentrations of albumin, bilirubin, and high-density lipoproteins were different ...
H G, Giles   +3 more
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Oestriol binding to plasma proteins

Journal of Steroid Biochemistry, 1988
Simple diffusion experiments indicated that oestriol was retained by human pregnancy plasma more effectively than by albumin solutions of a corresponding concentration. Oestriol bound (Ka = 6 X 10(6) l/mol at 4 degrees C) to a glycoprotein which had been isolated from plasma by adsorption to Concanavalin A.
V, Moutsatsou, R E, Oakey
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PLASMA RETINOL‐BINDING PROTEIN*

Annals of the New York Academy of Sciences, 1980
Vitamin A is mobilized from liver stores and transported in plasma in the form of the lipid alcohol retinol, bound to a specific transport protein, retinol-binding protein (RBP). A great deal is known about the chemical structure, metabolism, and biological roles of RBP. RBP is a single polypeptide chain with molecular weight close to 20,000.
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Plasma / Serum Protein Binding Determinations

Current Drug Metabolism, 2008
The binding of a drug to serum or plasma proteins enables the transport of drugs via the blood to sites of action throughout the body. For expediency we will use serum proteins throughout this discussion with the understanding that one can substitute the term plasma proteins in all experimental instances.
Michael J, Banker, Tracey H, Clark
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Plasma Steroid-Binding Proteins

Endocrinology and Metabolism Clinics of North America, 1991
Two steroid-binding proteins circulate in plasma, corticosteroid-binding globulin and sex hormone-binding globulin. They both have several different but connected, physiologic functions. Each is the major determinant of the concentration of the physiologically important hormones that they bind.
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Plasma Protein Binding of Challenging Compounds

Journal of Pharmaceutical Sciences, 2015
Accurately determining fraction unbound (fu ) with currently available methods has been challenging for certain compounds. Inaccurate fu values can lead to the misinterpretation of important attributes of a drug candidate. Our analysis of over 2000 Pfizer drug discovery compounds showed no systematic bias in low or high fu precision using the ...
Keith, Riccardi   +7 more
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Plasma Protein Binding of Gyrase Inhibitors

Journal of Pharmaceutical Sciences, 1998
Plasma protein binding of a wide range of gyrase inhibitors in clinical practice or trials has been determined by ultrafiltration to determine structure-protein binding relationships. The protein binding was independent of overall lipophilicity. In particular, the "western" part of the "quinolone" skeleton, consisting of a heterocyclus at position 7 ...
G, Zlotos   +4 more
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Enantioselective plasma protein binding of bimoclomol

Chirality, 2002
AbstractThe binding of bimoclomol enantiomers to human plasma, its components, as well as to plasma from monkey, dog, rat, and mouse was investigated by ultrafiltration and equilibrium dialysis. The considerably stronger binding of the (−)‐(S)‐enantiomer found in human plasma is due to the alpha1‐acid glycoprotein (AAG) component.
Júlia, Visy   +5 more
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