BIOHYBRID BRANCHED COPOLYMERS OF CONTROLLED NANOSTRUCTURE BASED ON POLYACRYLAMIDE GRAFTED TO DEXTRAN OR DEXTRAN SULPHATE BACKBONE

2008 ◽  
Author(s):  
N. Kutsevol ◽  
R. Soushko ◽  
J.-M. Guenet ◽  
N. Melnyk ◽  
Alberto D’Amore ◽  
...  
Keyword(s):  
Dextran Sulphate ◽  
Branched Copolymers

Studies on the Fibrinolytic System in Human Plasma: Quantitative Determination of Plasminogen Activators and Proactivators

1979 ◽  
Vol 41 (02) ◽  
pp. 365-383 ◽  
Author(s):  
C Kluft
Keyword(s):  
Pilot Study ◽  
Plasma Level ◽  
Human Plasma ◽  
Plasminogen Activators ◽  
Venous Occlusion ◽  
Quantitative Information ◽  
Optimal Recovery ◽  
Dextran Sulphate ◽  
Baseline Levels

SummaryEffects due to plasma plasminogen activators and proactivators are usually studied in assay systems where inhibitors influence the activity and where the degree of activation of proactivators is unknown. Quantitative information on activator and proactivator levels in plasma is therefore not availableStudies on the precipitating and activating properties of dextran sulphate in euglobulin fractionation presented in this paper resulted in the preparation of a fraction in which there was optimal recovery and optimal activation of a number of plasminogen activators and proactivators from human plasma. The quantitative assay of these activators on plasminogen-rich fibrin plates required the addition of flufenamate to eliminate inhibitors. The response on the fibrin plates (lysed zones) could be coverted to arbitrary blood activator units (BAU). Consequently, a new activator assay which enables one to quantitatively determine the plasma level of plasminogen activators and proactivators together is introduced.Two different contributions could be distinguished: an activity originating from extrinsic activator and one originating from intrinsic proactivators. The former could be assayed separately by means of its resistance to inhibition by Cl-inactivator. Considering the relative concentrations of extrinsic and intrinsic activators, an impression of the pattern of activator content in plasma was gained. In morning plasma with baseline levels of fibrinolysis, the amount of extrinsic activator was negligible as compared to the level of potentially active intrinsic activators. Consequently, the new assay nearly exclusively determines the level of intrinsic activators in morning plasma. A pilot study gave a fairly stable level of 100 ± 15 BAU/ml (n = 50). When fibrinolysis was stimulated by venous occlusion (15 min), the amount of extrinsic activator was greatly increased, reaching a total activator level of 249 ± 27 BAU/ml (n = 7).

Generation Of Factor XII-Dependent Plasminogen Activator Activity In Human Plasma Measured With A Fluorogenic Substrate

1981 ◽  
Author(s):  
G Dooijewaard ◽  
C Kluft
Keyword(s):  
Human Plasma ◽  
Plasminogen Activator ◽  
Minor Role ◽  
Factor Xii ◽  
Dextran Sulphate ◽  
Fluorogenic Substrate ◽  
A Value ◽  
Substrate Activation ◽  
Factor Xiia ◽  
A Minor

A rapid fluorometric assay for measurement of amidolytic activity in human plasma was developed, using the plasminogen activator sensitive synthetic substrate t-BOC-L-valyl--glycyl-L-arginine-β-naphthylamide. The plasma is diluted in a reaction cuvet containing 0.050 M Tris HC1 buffer (pH 8.0) and 150 μM substrate. Activation of plasminogen proactivator(s) is initiated at 37°C by the addition of 10 μg dextran sulphate (MW 500,000)/ml. The concentration of β-naphthyl- amide released is recorded fluorometrically as a function of time. The slope of this curve at any time t is proportional to the concentration of activator. Thus, in a single assay, the entire time-dependent profile of activation and subsequent inhibition is monitored; this provides 1. a value for an optimum plasminogen activator content in the plasma, and 2. the time it takes to reach the optimum. The plot of optimum activator content against μl of plasma added is linear for dilutions more than 100-fold, suggesting that under these conditions the optimum content approaches the content of proactivator(s) originally present.The activator content measured predominantly consists of contributions of a factor XII-dependent process since 1. without dextran sulphate or with plasmas deficient in factor XII or prekallikrein no activity could be generated, and 2. plots of optimum activator content against dextran sulphate concentration show sigmoidal-shaped saturation curves as found previously for the kallikrein generation in human plasma. Contributions of factor XIIa and kallikrein only partly account for the content measured and studies with plasmas deficient in factor XI point to a minor role for this factor, if any. Further identification of the activator (s) involved is in progress.

scholarly journals Detecting levels of polyquaternium-10 (PQ-10) via potentiometric titration with dextran sulphate and monitoring the equivalence point with a polymeric membrane-based polyion sensor

2016 ◽  
Vol 8 (29) ◽  
pp. 5806-5811 ◽  
Author(s):  
Stephen A. Ferguson ◽  
Xuewei Wang ◽  
Mark E. Meyerhoff
Keyword(s):  
Potentiometric Titration ◽  
Polymeric Membrane ◽  
Dextran Sulphate ◽  
Equivalence Point

This manuscript reports a novel and facile method for PQ-10/SLS separation and subsequent PQ-10 quantification via potentiometric titration.

A new flavonoid derivative, dosmalfate, attenuates the development of dextran sulphate sodium-induced colitis in mice

2003 ◽  
Vol 3 (13-14) ◽  
pp. 1731-1741 ◽  
Author(s):  
Isabel Villegas ◽  
Catalina Alarcón de la Lastra ◽  
Aurelio Orjales ◽  
Carmen La Casa
Keyword(s):  
Dextran Sulphate ◽  
Dextran Sulphate Sodium

Impact of dextran sulphate sodium-induced colitis on the intestinal transport of the colon carcinogen PhIP

2015 ◽  
Vol 90 (5) ◽  
pp. 1093-1102 ◽  
Author(s):  
Petra Nicken ◽  
Anne von Keutz ◽  
Ina Willenberg ◽  
Annika I. Ostermann ◽  
Nils Helge Schebb ◽  
...  
Keyword(s):  
Intestinal Transport ◽  
Dextran Sulphate ◽  
Dextran Sulphate Sodium
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