Preparation of Human Plasminogen Suitable as Substrate for Quantitative Determination of Plasminogen Activators

1966 ◽  
Vol 15 (03/04) ◽  
pp. 511-518
Author(s):  
W Berg ◽  
K Korsan-Bengtsen ◽  
J Ygge
Keyword(s):  
Ionic Strength ◽  
Quantitative Determination ◽  
Spontaneous Activity ◽  
Human Plasma ◽  
Gel Filtration ◽  
Plasminogen Activators ◽  
Simple Method ◽  
Neutral Ph ◽  
Human Plasminogen

SummaryA simple method for preparation of plasminogen with low spontaneous activity and soluble at a neutral pH and at physiological ionic strength is described. Euglobulin made from fresh, oxalated, BaSO4-adsorbed, human plasma was first purified by means of gel filtration on Sephadex G-200. After gel filtration, further purification and concentration was done on DEAE-sephadex A-50. The activity was 100-130 casein units per mg tyrosine.

Simplified Determination of Fibrinogen Subfractions by Glycine

1979 ◽  
Author(s):  
S. Sasaki ◽  
K. Kito
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Human Plasma ◽  
Gel Electrophoresis ◽  
Biological Properties ◽  
Strength Analysis ◽  
Simple Method ◽  
Molecular Fraction ◽  
The Difference

Although it has been suggested by some investigators that human plasma fibrinogen is composed of two or more subfractions, no simple method of determining these fractions individually has been available for clinical use. We found that precipitation by glycine at certain ionic strength was suitable for this purpose. One volume of human plasma was added to 10 volume of 2.3 M glycine solution of varying ionic strength. Analysis of the precipitates obtained at various Ionic strength by means of SDS-gel electrophoresis gave the following results: The precipitate obtained at ionic strength 0.2 gave single band. Its molecular weight was 360,000, clottability 85%. The supernatant was devoid of this fraction. The precipitate obtained at ionic strength 1.4 gave two banda corresponding to molecular weight of 360,000 and 325,00O respectively. The clottability of the precipitate was 85%. The supernatant contained no significant amount of clottable protein. It is therefore possible to determine the concentrations of high molecular fraction of fibrinogen and of total fibrinogen in plasma using the precipitate at ionic strength 0.2 and the precipitate at ionic strength 1.4 respectively. The difference of the two values gives the concentration of low molecular fraction of fibrinogen. Biological properties of the two fractions were also studied.

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).

Comparative Study of Proactivators of the Fibrinolysin System in Three Mammalian Species

1969 ◽  
Vol 21 (03) ◽  
pp. 594-603 ◽  
Author(s):  
Y Takada ◽  
A Takada ◽  
J. L Ambrus
Keyword(s):  
Guinea Pig ◽  
Comparative Study ◽  
Human Plasma ◽  
Mammalian Species ◽  
Gel Filtration ◽  
Plasminogen Activators ◽  
The Other ◽  
Rabbit Plasma ◽  
Plate Test ◽  
Fibrin Plate

SummarySephadex gel filtration of human plasma gave results suggesting the presence of two proactivators of plasminogen, termed proactivators A and B.Activity resembling that of proactivator A was found in rabbit plasma, but not in guinea pig plasma.Plasminogen activators produced by the interaction of proactivator A of human plasma with streptokinase had no caseinolytic or TAMe esterolytic effect.Proactivator A can be separated in a form apparently free from plasminogen, as shown by the heated fibrin plate test and by immunological analysis. On the other hand, proactivator B concentrates prepared so far are contamined with plasminogen.Human proactivators appear to be far more susceptible to streptokinase than are rabbit proactivators.Inhibitors of the fibrinolysin system were observed in the plasmas of all 3 species. These inhibitors are not present in the euglobulin fraction of plasma. Sephadex fractionation of euglobulin fractions results in proactivator preparations that do not contain inhibitors.

scholarly journals Recovery of Hg(0) from the Aqueous Hg(I/II) Present in Analyte Solution after Quantitative Determination of Iron

2013 ◽  
Vol 2013 ◽  
pp. 1-3
Author(s):  
Suman K. Giri ◽  
Nigamananda Das
Keyword(s):  
Aqueous Solutions ◽  
Quantitative Determination ◽  
Simple Method ◽  
Stoichiometric Amount ◽  
Analyte Solution

An easy and feasible approach to recover HgCl2, used in quantitative determination of iron values, as Hg(0) was described. Both Hg(I) and Hg(II), present in the solution after quantitative determination of iron, was completely reduced to Hg(0) by the addition of aluminium chips in more slightly excess than the stoichiometric amount. The purity of recovered Hg(0) was verified by comparing the value of density with pure mercury. This simple method may be useful to remove the mercury from other waste aqueous solutions before their discharge into the environment.

Quantitative Determination of Progesterone in Human Plasma by Thin-Layer and Gas-Liquid Radiochromatography

Nature ◽  
1964 ◽  
Vol 203 (4947) ◽  
pp. 836-839 ◽  
Author(s):  
WILLIAM P. COLLINS ◽  
IAN F. SOMMERVILLE
Keyword(s):  
Thin Layer ◽  
Quantitative Determination ◽  
Human Plasma
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