Results 301 to 310 of about 1,940,722 (375)

Lidocaine plasma protein binding

Clinical Pharmacology and Therapeutics, 1980
The percent of unbound lidocaine in the plasma of 24 healthy subjects was measured by equilibrium dialysis after addition of 3 microgram/ml C14 lidocaine hydrochloride. The percentage of unbound lidocaine varied from 19.9 to 38.8 (30.2 +/- 5, mean +/- SD) was inversely related to the concentration of alpha 1-acid glycoprotein (AAG) in the plasma (r ...
Barbara B. Kitchell, Thorir D. Bjornsson, David G. Shand, Philip A. Routledge, Aaron Barchowsky   +4 more
openaire   +3 more sources

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 ...
William A. Corrigall, H. G. Giles, V Khouw, Edward M. Sellers   +3 more
openaire   +3 more sources

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.
openaire   +3 more sources

Determination of atypical nonlinear plasma−protein-binding behavior of tigecycline using an in vitro microdialysis technique.

Journal of Pharmacy and Science, 2014
Tigecycline, a novel glycylcycline antibiotic, shows atypical nonlinear plasma-protein-binding behavior using ultrafiltration and ultracentrifugation techniques. The mechanism of such counterintuitive behavior is currently unknown.
J. Mukker, R. Singh, H. Derendorf
semanticscholar   +1 more source

Rational use of plasma protein and tissue binding data in drug design.

Journal of Medicinal Chemistry, 2014
It is a commonly accepted assumption that only unbound drug molecules are available to interact with their targets. Therefore, one of the objectives in drug design is to optimize the compound structure to increase in vivo unbound drug concentration.
Xingrong Liu, M. Wright, C. Hop
semanticscholar   +1 more source

Plasma protein binding: from discovery to development.

Journal of Pharmacy and Science, 2013
The importance of plasma protein binding (PPB) in modulating the effective drug concentration at pharmacological target sites has been the topic of significant discussion and debate amongst drug development groups over the past few decades.
T. Bohnert, L. Gan
semanticscholar   +1 more source

The plasma protein binding of HIDA

European Journal of Nuclear Medicine, 1980
By using Sephadex gel column chromatography to separate substances into their various components according to molecular weight, we have investigated the effect of incubating several "brands" of HIDA in plasma, in vitro. The results show that such incubation has no effect on either dimethyl HIDA, or diethyl HIDA, but that in the case of para-butyl HIDA,
R. W. Nicholson, R. A. Shields, K. J. Herman, H. J. Testa   +3 more
openaire   +3 more sources

Species differences in drug plasma protein binding

, 2014
Comparison of the human plasma protein binding data for a variety of drug discovery compounds indicates that compounds tend to be slightly more bound to human plasma proteins, than compared to plasma proteins from rats, dogs or mice.
N. Colclough, Linette Ruston, J. M. Wood, P. Macfaul   +3 more
semanticscholar   +1 more source

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.
R.E. Oakey, V. Moutsatsou
openaire   +3 more sources

The binding of cortisol by plasma protein

Archives of Biochemistry and Biophysics, 1958
Abstract When plasma cortisol concentrations are less than 30 μg./100 ml., the steroid is tightly bound by protein and cannot be ultrafiltered. When the concentration is raised higher than 40 μg./100 ml., either by addition of exogenous cortisol in vitro or as a result of the effects of adrenocorticotropic hormone (ACTH) or of sickness on the ...
G. Virginia Upton, Philip K. Bondy
openaire   +3 more sources