The binding of the antimalarial arteether to human plasma proteins in-vitro

1992 ◽  
Vol 44 (11) ◽  
pp. 940-942 ◽  
Author(s):  
S. Wanwimolruk ◽  
G. Edwards ◽  
S. A. Ward ◽  
A. M. Breckenridge
Keyword(s):  
Human Plasma ◽  
Plasma Proteins

362 Binding of gefitinib (ZD1839) to human plasma proteins: in vitro and clinical pharmacokinetic (PK) studies

2004 ◽  
Vol 2 (8) ◽  
pp. 109
Author(s):  
J. Li ◽  
J. Brahmer ◽  
W. Messersmith ◽  
M. Hidalgo ◽  
S.D. Baker
Keyword(s):  
Human Plasma ◽  
Clinical Pharmacokinetic ◽  
Plasma Proteins

scholarly journals Some Physiological Factors Affecting the Binding of Cortisol by Human Plasma Proteins

1977 ◽  
Vol 14 (1-6) ◽  
pp. 35-38 ◽  
Author(s):  
J. D. Few ◽  
J. R. Haspineall
Keyword(s):  
Steady State ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Gel Filtration ◽  
Physiological Factors ◽  
Mean Values ◽  
Factors Affecting ◽  
Free Cortisol ◽  
The Mean

Steady-state gel filtration has been used to study the binding of cortisol to human plasma proteins in vitro. Raising the temperature from 37°C to 41°C results in the mean proportion of free (non-protein-bound) cortisol rising approximately from 7% to 11%. Addition of cortisol to plasma ≡ 275 nmol/l) also increased the proportion of free cortisol by approximately 50%. Cortisone is less strongly bound to plasma proteins than cortisol. The mean values (±S.D.) for five samples were free cortisol 8.4 ± 1.1% and free cortisone 26.0±3.8%.

scholarly journals Interaction of prostaglandins with blood plasma proteins. Comparative binding of prostaglandins A2, F2α and E2 to human plasma proteins

1972 ◽  
Vol 130 (2) ◽  
pp. 631-636 ◽  
Author(s):  
Amiram Raz
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Prostaglandin F2α ◽  
Association Constants ◽  
Comparative Binding ◽  
Blood Plasma Proteins ◽  
Prostaglandin A2 ◽  
Apparent Association

1. The binding of prostaglandin A2 and prostaglandin F2α to human plasma proteins was investigated by DEAE-Sephadex chromatography and polyacrylamide-gel electrophoresis. Both prostaglandins, when added to human plasma in vitro, were found to become bound mainly to plasma albumin. 2. The extent of binding of prostaglandins added to human plasma in low to moderate concentrations was found to be approx. 88, 73 and 58% for prostaglandins A2, E2 and F2α respectively. The order of affinities for the binding of the three prostaglandins to albumin appear to be A2>E2>F2α. 3. The apparent association constants for the binding of these prostaglandins to human serum albumin were estimated to be approx. 4.8×104, 2.4×104 and 0.9×104 litre/mol for prostaglandins A2, E2 and F2α respectively. The results are compared with previously reported association constants for the binding of long-chain fatty acids to both human and bovine albumins.

scholarly journals The protective effects of selenoorganic compounds against peroxynitrite-induced changes in plasma proteins and lipids

2006 ◽  
Vol 11 (1) ◽  
pp. 1-11 ◽  
Author(s):  
Paweł Nowak ◽  
Joanna Saluk-Juszczak ◽  
Beata Olas ◽  
Joanna Kołodziejczyk ◽  
Barbara Wachowicz
Keyword(s):  
Lipid Peroxidation ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Enzyme Inhibitors ◽  
Group Formation ◽  
Plasma Lipid ◽  
Protective Effects ◽  
Induced Changes ◽  
Plasma Lipid Peroxidation

AbstractMany selenoorganic compounds play an important role in biochemical processes and act as antioxidants, enzyme inhibitors or drugs. The effects of a new selenocompound — bis(2-aminophenyl)-diselenide on oxidative/nitrative changes in human plasma proteins induced by peroxynitrite (ONOO−) were studied in vitro and compared with the those of ebselen, a well-known antioxidant. We also studied the role of the tested selenocompounds in peroxynitrite-induced plasma lipid peroxidation. Exposure of the plasma to peroxynitrite (0.1 mM) resulted in an increase in the level of carbonyl groups and nitrotyrosine residues in plasma proteins (estimated using the ELISA method and Western blot analysis). In the presence of different concentrations (0.025–0.1 mM) of the tested selenocompounds, 0.1 mM peroxynitrite caused a distinct decrease in the level of carbonyl group formation and tyrosine nitration in plasma proteins. Moreover, these selenocompounds also inhibited plasma lipid peroxidation induced by ONOO−1 (0.1 mM). The obtained results indicate that in vitro bis(2-aminophenyl)-diselenide and ebselen have very similar protective effects against peroxynitrite-induced oxidative/nitrative damage to human plasma proteins and lipids.

In vitro studies on the binding of cloprednol to human plasma proteins

1982 ◽  
Vol 16 (1) ◽  
pp. 75-80 ◽  
Author(s):  
R.V. Tomlinson ◽  
R. Runkel ◽  
M.D. Chaplin ◽  
L. Bowen ◽  
J. Kanagy ◽  
...  
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
In Vitro Studies

scholarly journals Interaction of Camptothecin Derivatives with Human Plasma Proteins in Vitro

1993 ◽  
Vol 113 (2) ◽  
pp. 167-175 ◽  
Author(s):  
Yukihisa KURONO ◽  
Makoto MIYAJIMA ◽  
Ken IKEDA
Keyword(s):  
Human Plasma ◽  
Plasma Proteins

Immunoenzymatic demonstration of the simultaneous presence of transferrin, hemopexin and albumin in a same hepatocyte and their ultrastructural localization

1978 ◽  
Vol 36 (2) ◽  
pp. 88-89
Author(s):  
M. Kraemer ◽  
J. Foucrier ◽  
J. Vassy ◽  
M.T. Chalumeau
Keyword(s):  
Plasma Proteins ◽  
Rat Hepatocytes ◽  
Ultrastructural Localization ◽  
Carrier Proteins ◽  
Normal Cells ◽  
Adult Rat ◽  
Adult Rat Hepatocytes ◽  
Monospecific Antisera ◽  
Different Levels

Some authors using immunofluorescent techniques had already suggested that some hepatocytes are able to synthetize several plasma proteins. In vitro studies on normal cells or on cells issued of murine hepatomas raise the same conclusion. These works could be indications of an hepatocyte functionnal non-specialization, meanwhile the authors never give direct topographic proofs suitable with this hypothesis.The use of immunoenzymatic techniques after obtention of monospecific antisera had seemed to us useful to bring forward a better knowledge of this problem. We have studied three carrier proteins (transferrin = Tf, hemopexin = Hx, albumin = Alb) operating at different levels in iron metabolism by demonstrating and localizing the adult rat hepatocytes involved in their synthesis.Immunological, histological and ultrastructural methods have been described in a previous work.

Investigation of the Free and Total Thyroxine-binding Capacity of Plasma Proteins in Thyroid Disorders

1971 ◽  
Vol 10 (04) ◽  
pp. 299-304
Author(s):  
József Takó ◽  
János Fischer ◽  
Jusztina Juhász ◽  
Ilona Sztraka ◽  
István Kapus ◽  
...  
Keyword(s):  
Blood Cell ◽  
Thyroid Function ◽  
Oral Contraceptives ◽  
Red Blood Cell ◽  
Plasma Proteins ◽  
Binding Capacity ◽  
Thyroid Disorders ◽  
Thyroid Function Tests ◽  
Total Thyroxine

SummaryThe results of thyroid function tests have been compared with data on the thyroxine-binding capacity of plasma proteins in hyper-, hypo- and euthyroid cases, the latter including women taking oral contraceptives (Infecundin). It was found that there exists a significant correlation of exponential nature between the in vitro red blood cell 125I-triiodothyronine uptake (RCU) and the free thyroxine-binding capacity of the thyroxine-inding globulin (TBG).

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