The Effects of Sodium Citrate and an Excess of Plasminogen on Fibrinolytic Agents

1960 ◽  
Vol 04 (03) ◽  
pp. 462-472 ◽  
Author(s):  
Tage Astrup ◽  
Ida Sterndorff
Keyword(s):  
Fumaric Acid ◽  
Maleic Acid ◽  
Fibrinolytic Activity ◽  
Sodium Citrate ◽  
Plasminogen Activators ◽  
Fibrinolytic Agents ◽  
Enhancing Effect ◽  
Polycarboxylic Acids

Summary1. The presence of citrate in the normal fibrin enhanced the fibrinolytic activity of plasminogen activators, including trypsin. The effect of proteases (on normal or on heated fibrin, containing citrate) was not significantly influenced.2. The effect of plasminogen activators was also increased when excess of plasminogen was present in the normal fibrin plates.3. Fumaric acid and maleic acid belong to the polycarboxylic acids producing an enhancing effect.

Interaction of Heparin with Fibrinolysis

1963 ◽  
Vol 09 (02) ◽  
pp. 446-458 ◽  
Author(s):  
Rudolf Holemans ◽  
Dionysios Adamis ◽  
James F Horace
Keyword(s):  
Human Plasma ◽  
Fibrinolytic Activity ◽  
Plasminogen Activation ◽  
Fibrinolytic Agents ◽  
High Concentration ◽  
Enhancing Effect

SummaryHeparin in high concentration inhibits the fibrinolysis of human plasma clots or bovine fibrin by fibrinolytic agents which produce plasminogen activation. Heparin has no effect on the fibrinolytic activity of plasmin or Aspergillus protease.In order to produce inhibition of plasminogen activation heparin requires the presence of a co-factor which is present in citrated human plasma but absent from its euglobulin fraction.In none of the concentrations tested has heparin an enhancing effect on fibrinolysis.

New assay of fibrinolytic activity as a continuous rate reaction

1970 ◽  
Vol 48 (1) ◽  
pp. 61-68 ◽  
Author(s):  
Walter H. E. Roschlau ◽  
Sandra L. Miller
Keyword(s):  
Fibrinolytic Activity ◽  
Enzymatic Degradation ◽  
Proteolytic Enzymes ◽  
Plasminogen Activators ◽  
Light Transmittance ◽  
Plasminogen Activation ◽  
Fibrinolytic Agents ◽  
Vitro Assay ◽  
Relative Potencies

A new and rapidly performed in vitro assay of fibrinolytic activity, incorporating turbidimetric measurements of fibrin suspension substrate, is described. The assay allows the write-out of rate reactions by recording the changes in light transmittance through a sample of substrate while it is subjected to enzymatic degradation by fibrinolytic agents. By running the reaction in buffer or serum, the properties of plasminogen activators can be differentiated from those of proteolytic enzymes. Data obtained with this method allow the estimation of relative potencies, quantitative inhibition of enzymes by serum, rate of plasminogen activation, etc., for which examples are given.

A Comparative Ex Vivo Study of Plasminogen Activators and Proteases for Fibrinolytic Activity and Side Effects in Rabbits

1977 ◽  
Vol 37 (01) ◽  
pp. 154-161 ◽  
Author(s):  
B. A Janik ◽  
S. E Papaioannou
Keyword(s):  
Side Effects ◽  
Effective Dose ◽  
Fibrinolytic Activity ◽  
Ex Vivo ◽  
Plasminogen Activators ◽  
Assay System ◽  
Coagulation Parameters ◽  
Ex Vivo Assay

SummaryUrokinase, streptokinase, Brinase, trypsin, and SN 687, a bacterial exoprotease, have been evaluated in an ex vivo assay system. These enzymes were injected into rabbits and the fibrinolytic activity as well as other coagulation parameters were measured by in vitro techniques. Dose-response correlations have been made using the euglobulin lysis time as a measure of fibrinolytic activity and the 50% effective dose has been determined for each enzyme. Loading doses, equal to four times the 50% effective dose, were administered to monitor potential toxicity revealing that Brinase, trypsin, and SN 687 were very toxic at this concentration.Having established the 50% effective dose for each enzyme, further testing was conducted where relevant fibrinolytic and coagulation parameters were measured for up to two days following a 50% effective dose bolus injection of each enzyme. Our results have demonstrated that urokinase and streptokinase are plasminogen activators specifically activating the rabbit fibrinolytic system while Brinase, trypsin and SN 687 increase the general proteolytic activity in vivo.The advantages of this ex vivo assay system for evaluating relative fibrinolytic potencies and side effects for plasminogen activators and fibrinolytic proteases have been discussed.

Effect of Bentonite on Fibrinolytic System in Serum

1963 ◽  
Vol 10 (01) ◽  
pp. 120-132 ◽  
Author(s):  
E. S Olesen
Keyword(s):  
Guinea Pig ◽  
Plasminogen Activator ◽  
Fibrinolytic Activity ◽  
High Potential ◽  
Fibrinolytic System ◽  
Fibrinolytic Agents ◽  
Isoelectric Precipitation ◽  
Active Protease ◽  
Pig Serum

SummaryTreatment of serum with bentonite led to a reduced content of inhibitors of trypsin and urokinase in the isoelectrically precipitated euglobulin, and removed fibrinolytic agents and precursors from serum. Bentonite-treated serum added to untreated serum reduced precipitation of the above inhibitors, and presumably also precipitation of inhibitors against a plasminogen activator of serum.Bentonite-treated serum (whether from pig, ox, guinea-pig, or man), added to untreated guinea-pig serum, produced fibrinolytic activity on isoelectric precipitation of the mixture; the activity of the euglobulin was due to an activator of plasminogen as well as an active protease, probably plasmin. The described effects of bentonite-treated serum are similar to those previously reported for anionic polyelectrolytes. Possible mechanisms are discussed.The “non-specific” activation of fibrinolytic activity by means of bentonite emphasizes that guinea-pig serum [which is characterized by a high potential for “nonspecific” activation of its fibrinolytic system Olesen (1962)] contains all the elements required for the formation of an activator of plasminogen, and thus the activation of its plasminogen to plasmin.

scholarly journals THEORETICAL STUDY OF THE ISOMERIZATION OF MALEIC ACID INTO FUMARIC ACID

2011 ◽  
Vol 56 (2) ◽  
pp. 656-662 ◽  
Author(s):  
RICARDO UGARTE ◽  
CARLOS BUSTOS ◽  
IGNACIO MORENO-VILLOSLADA
Keyword(s):  
Fumaric Acid ◽  
Maleic Acid ◽  
Theoretical Study

Electrochemical Reduction Behaviors of Maleic Acid and Fumaric Acid at Lead Electrode

2008 ◽  
Vol 24 (07) ◽  
pp. 1264-1270
Author(s):  
SHAO Heng ◽  
◽  
◽  
GAN Yong-Ping ◽  
HUANG Hui ◽  
...  
Keyword(s):  
Electrochemical Reduction ◽  
Fumaric Acid ◽  
Maleic Acid ◽  
Lead Electrode

Fibrinolytic Agents

2006 ◽  
Author(s):  
Richard C. Becker ◽  
Frederick A. Spencer
Keyword(s):  
Body Weight ◽  
Patient Management ◽  
Factor Viia ◽  
Plasminogen Activators ◽  
Common Complication ◽  
Fibrinolytic Agents ◽  
Life Threatening ◽  
Potential Factor ◽  
Tissue Factor Pathway ◽  
High Concentrations

The generation of plasmin from plasminogen by plasminogen activators (fibrinolytic agents) induces a variety of effects in addition to dissolving fibrin strands, degrading fibrinogen, and inhibiting tissue factor pathway and factor VIII. It also, in high concentrations, causes platelet activation. Thus, fibrinolytic agents have both prothrombotic and antihemostatic properties—the latter of which is often augmented by the concomitant use of anticoagulants and platelet antagonists (see Chapter 12). Bleeding is the most common complication of fibrinolytic (and adjunctive antithrombotic) therapy. The most important predictors of nonintracranial hemorrhage are older age, invasive procedures, low body weight, and female sex (de Jaegre et al, 1992; GISSI 2 Investigators, 1990; GUSTO-III Investigators, 1997; INJECT Investigators, 1995). Predictors of intracranial hemorrhage include age (>65 years), low body weight (<70 kg), hypertension on admission, and alteplase (vs. streptokinase) (GUSTO-III Investigators, 1997). The approach to patient management in cases of fibrinolytic-induced bleeding is summarized in Figure 30.1. It is important to consider antithrombotic agents that may concomitantly increase hemorrhagic potential. Factor VIIa (recombinant; NovoSeven) represents a treatment alternative for life-threatening hemorrhagic complications.

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