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.

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%.

A comparative binding of platinum anti-tumour compounds to plasma proteins in the rat (in vivo) and mouse (in vitro)

1992 ◽  
Vol 85 (2-3) ◽  
pp. 199-213 ◽  
Author(s):  
Anusha Perera ◽  
Harold Jackson ◽  
Harbans L. Sharma ◽  
Charles A. McAuliffe ◽  
Brian W. Fox
Keyword(s):  
Plasma Proteins ◽  
Comparative Binding

scholarly journals Protective action of carnosine and organic lithium salts in case of ethanol-induced oxidative damage of proteins and lipids of blood plasma in healthy persons and alcoholic patients

2019 ◽  
Vol 65 (1) ◽  
pp. 28-32 ◽  
Author(s):  
V.D. Prokopieva ◽  
E.V. Plotnikov ◽  
E.G. Yarygina ◽  
N.A. Bokhan
Keyword(s):  
Blood Plasma ◽  
Plasma Proteins ◽  
Protective Action ◽  
Lithium Carbonate ◽  
Lithium Salts ◽  
Oxidized Proteins ◽  
Blood Plasma Proteins ◽  
Healthy Persons ◽  
In Blood Plasma

Organic lithium salts containing anionic components (succinate, fumarate, pyruvate and antioxidant ascorbate) were tested for protection of blood plasma proteins and lipids against ethanol-induced oxidation in vitro. We used normothymic lithium carbonate and well-known antioxidant dipeptide carnosine (b-alanyl-L-histidine) as the reference drugs. The oxidized proteins and lipids were determined by the level of carbonylated proteins (CP) and TBA-reactive products (TBA-RP), respectively. In alcoholic patients the level of oxidized proteins and lipids was higher than in healthy persons. Incubation of blood with ethanol resulted in an increase in oxidized proteins and lipids in blood plasma of healthy persons but had no influence on the level of CP and TBA-RP in blood plasma of alcoholic patients. Lithium carbonate, lithium ascorbate, and lithium succinate exhibited protective action against ethanol-induced oxidation of biomolecules of blood plasma of healthy people. These effects were comparable with carnosine action. The studied compounds had no effect on the level of CP and TBA-RP of blood plasma of alcoholic patients.

scholarly journals Complex-formation and inhibition of urokinase by blood plasma proteins

1983 ◽  
Vol 215 (1) ◽  
pp. 123-131 ◽  
Author(s):  
E K Waller ◽  
W D Schleuning ◽  
E Reich
Keyword(s):  
Complex Formation ◽  
Rate Constant ◽  
Plasma Proteins ◽  
Proteinase Inhibitors ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Order Rate Constant ◽  
Reducing Conditions ◽  
Blood Plasma Proteins

We have studied the formation of covalent complexes between 125I-urokinase (125I-UK) and proteins in human plasma. Although 125I-UK reacts with many proteinase inhibitors in purified systems, the predominant complexes formed in plasma are with antithrombin III (ATIII) and alpha 2-macroglobulin (alpha 2M). 125I-UK interacts with purified alpha 2M or alpha 2M in plasma to form a characteristic pattern of multiple complexes whose Mr values by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis are in the range of 380 000-720 000, under non-reducing conditions, and 180 000-430 000 after reduction. We also examined the inhibition of UK amidolytic activity by plasma and by purified ATIII. In the presence of saturating concentrations of ATIII and heparin, an apparent first-order rate constant of 6.8 X 10(-1) s-1 was calculated for the inhibition of urokinase. In contrast, the rate constant for the formation of covalent ATIII-UK complexes was lower, suggesting the inhibition of UK proceeds first via the formation of transient non-covalent intermediates that are then transformed more slowly into covalent end products. The observed rate constants for enzyme inhibition or complex-formation with plasma or purified inhibitors are insufficient to account for the reported clearance rate of injected UK in vivo.

scholarly journals Lipoprotein-Associated Phospholipase A2 Activity Is a Marker of Small, Dense LDL Particles in Human Plasma

2005 ◽  
Vol 51 (12) ◽  
pp. 2264-2273 ◽  
Author(s):  
Irene Gazi ◽  
Evangelia S Lourida ◽  
Theodosios Filippatos ◽  
Vasilis Tsimihodimos ◽  
Moses Elisaf ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Human Plasma ◽  
Polyacrylamide Gel Electrophoresis ◽  
Serum Triglyceride ◽  
Total Plasma ◽  
Pla2 Activity ◽  
Ldl Particles ◽  
Mass Proportion ◽  
Ldl Subfractions

Abstract Background: Recent clinical studies showed that lipoprotein-associated phospholipase A2 (Lp-PLA2) is a predictor for incident atherosclerotic disease. We have previously shown that among the LDL subfractions, Lp-PLA2 activity is preferentially associated with the atherogenic small, dense (sdLDL) particles in vitro. We investigated whether Lp-PLA2 could be a marker of sdLDL in human plasma. Methods: One hundred and seventy-six individuals participated in the study. LDL subclass analysis was performed by polyacrylamide gel electrophoresis. Lp-PLA2 activity and mass were determined in total plasma and in apolipoprotein B-depleted plasma (HDL-Lp-PLA2). Non–HDL-Lp-PLA2 activity and mass were calculated by subtracting the HDL-Lp-PLA2 from total plasma Lp-PLA2. Results: On the basis of the LDL subclass analysis, participants were categorized into phenotype A and non-A (total cholesterol mass of the sdLDL subfractions ≤0.155 and >0.155 mmol/L, respectively). Unlike total plasma Lp-PLA2 mass, total plasma Lp-PLA2 activity and non–HDL-Lp-PLA2 activity and mass were significantly higher in persons with phenotype non-A compared with persons with phenotype A, whereas HDL-Lp-PLA2 activity and mass were lower in persons with phenotype non-A compared with phenotype A. Total plasma activity and non–HDL-Lp-PLA2 activity and mass, but not Lp-PLA2 mass, were correlated with sdLDL-cholesterol mass, proportion, and mean LDL particle size. In multiple regression analysis, total plasma and non–HDL-Lp-PLA2 activities were the second best predictors of the presence of sdLDL particles in human plasma after serum triglyceride concentrations. At serum triglyceride concentrations >1.356 mmol/L, total plasma and non–HDL-Lp-PLA2 activity added significantly to the prediction of the presence of sdLDL in plasma. Conclusions: Lp-PLA2 activity, but not the enzyme mass, is a marker of sdLDL in human plasma.

Phosphorylation of human and rat blood plasma proteins in vitro with cyclic 3′,5′-AMP-stimulated protein kinase and [32 P]ATP

FEBS Letters ◽  
1981 ◽  
Vol 131 (1) ◽  
pp. 132-136 ◽  
Author(s):  
Elisabet Humble ◽  
Per-Olof Forsberg ◽  
Gunnel Bergström ◽  
Bror Edlund ◽  
Lorentz Engström
Keyword(s):  
Protein Kinase ◽  
Blood Plasma ◽  
Plasma Proteins ◽  
Rat Blood ◽  
Blood Plasma Proteins

BINDING OF 5α-ANDROSTANE-3α,17β-DIOL TO HUMAN PLASMA PROTEINS

1973 ◽  
Vol 57 (2) ◽  
pp. 289-298 ◽  
Author(s):  
A. F. CLARK ◽  
C. E. BIRD
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Association Constant ◽  
Equilibrium Dialysis ◽  
Paper Electrophoresis ◽  
Mean Value ◽  
Albumin Fraction ◽  
The Mean ◽  
Apparent Association ◽  
Apparent Association Constant

SUMMARY The binding of 5α-androstane-3α,17β-diol to human plasma proteins was studied by equilibrium dialysis. The mean value of 96·6% for men was significantly less than that of 97·5% for women. These values are higher than those found for 5α-dihydrotestosterone (95·0 and 97·3%, respectively) and for testosterone (92·4 and 95·3%, respectively). When the distribution of labelled steroid in the different protein fractions was studied by paper electrophoresis, male plasma showed a larger fraction of 5α-androstane-3α,17β-diol radioactivity in the albumin fraction and less in the β-globulin area than did female plasma. Similar finding were made when 5α-dihydrotestosterone was studied. No inter-α-globulin peak of radioactivity was found for 5α-androstane-3α,17β-diol and 5α-dihydrotestosterone as occurs for testosterone. Albumin binds more 5α-androstane-3α,17β-diol than 5α-dihydrotestosterone or testosterone when studied by equilibrium dialysis and this is due to a higher apparent association constant between albumin and the dihydroxysteroid.

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