Results 321 to 330 of about 2,396,679 (391)
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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

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   +3 more
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   +3 more
openaire   +3 more sources

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

Quantitative structure--plasma protein binding relationships of acidic drugs.

Journal of Pharmacy and Science, 2012
One of the most important factors, affecting significantly the overall pharmacokinetic and pharmacodynamic profile of a drug, is its binding to plasma protein (PPB).
Z. Zhivkova, I. Doytchinova
semanticscholar   +1 more source

Binding Affinities of Thyroxine-Binding Proteins in Turtle Plasma

General and Comparative Endocrinology, 1993
Binding affinities (Ka) for thyroxine (T4) by blood plasma and purified plasma proteins from two turtles, the slider (Trachemys scripta) and snapper (Chelydra serpentina), were compared with those of a human using equilibrium dialysis. The purified T4 binding protein (TBP) from T.
Karen A. Glennemeier, Paul Licht
openaire   +3 more sources

Mn++ BINDING BY PLASMA PROTEINS

International Journal of Peptide and Protein Research, 1973
54Mn2+ added to human or rabbit plasma in vitro combines selectively with the albumin fraction. At pH 7.0, the Scatchard plot yields a curve that may be resolved for two classes of sites: one, where n1 = 1 and K1 = 2.4 × 104, the other where n2 = 0.5 and K2 = 0.5 × 103.Zn2+, Ni2+ and Co2+ can compete effectively for these sites.
Arvind K.N. Nandedkar   +2 more
openaire   +3 more sources

Renin binding proteins in plasma

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1979
Renin is found in mouse plasma as high molecular weight forms, in addition to the fully active 40 000 dalton form. By using freshly 125 I-labelled 40 000 dalton pure submaxillary mouse renin, no binding to plasma proteins was demonstrable. However, unfolding and refolding of the labelled renin by guanidine facilitated binding to specific mouse and ...
Christian Malling   +4 more
openaire   +3 more sources

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