Sensitization of Stabilized Fibrin to Urea Dispersion by Undiluted Plasma and Serum

1977 ◽  
Vol 58 (2) ◽  
pp. 79-83 ◽  
Author(s):  
F. de Cataldo ◽  
F. Baudo
Keyword(s):  
Stabilized Fibrin

Characterization of soluble, FSF-stabilized fibrin complexes with special reference to the role of fibrinogen

1974 ◽  
Vol 5 (1) ◽  
pp. 21-32 ◽  
Author(s):  
Bernt Ly ◽  
Peter Kierulf ◽  
Erling Jakobsen ◽  
Karl Gravem
Keyword(s):  
Special Reference ◽  
Stabilized Fibrin

scholarly journals The Fate of Soluble Fibrin Monomer in Relation to Intravascular Fibrin Formation and Degradation in Rabbits

Blood ◽  
1974 ◽  
Vol 44 (5) ◽  
pp. 723-733 ◽  
Author(s):  
Victor Gurewich ◽  
Robert Wetmore ◽  
Andrzej Nowak ◽  
Boguslaw Lipinski
Keyword(s):  
Reticuloendothelial System ◽  
Radioactive Material ◽  
Fibrin Deposition ◽  
Rapid Loss ◽  
Major Pathway ◽  
Fibrin Formation ◽  
Fibrin Monomer ◽  
Subsequent Degradation ◽  
Stabilized Fibrin ◽  
Blood Radioactivity

Abstract 125I-labeled fibrinogen or fibrin monomer (FM) were infused into rabbits, and the radioactivity in the blood, certain organs, and urine was followed. In the FM rabbits, a progressive, relatively rapid loss of blood radioactivity occurred which was accompanied by radioactive deposits in the organs and the excretion of radioactivity in the urine. Extraction of radioactive material from homogenized organ tissues of FM-infused rabbits showed that most of it had the characteristics of stabilized fibrin. Administration of EACA did not change any of the measurements in the fibrinogen animals but increased the rate and extent of fibrin deposition in the FM animals. In animals made leukopenic with HN2, fibrin deposition was inhibited. The findings indicate that a major pathway of FM clearance from the blood involves fibrin formation and deposition with subsequent degradation and excretion. The reticuloendothelial system appeared to play a major role in FM clearance, since most of the fibrin deposits were found in the liver, and the highest concentration was in the spleen. A nonenzymatic mechanism of fibrin formation from soluble FM involving leukocytes is postulated.

scholarly journals Recombinant Destabilase from Hirudo medicinalis Is Able to Dissolve Human Blood Clots In Vitro

2021 ◽  
Vol 43 (3) ◽  
pp. 2068-2081
Author(s):  
Pavel Bobrovsky ◽  
Valentin Manuvera ◽  
Izolda Baskova ◽  
Svetlana Nemirova ◽  
Alexandr Medvedev ◽  
...  
Keyword(s):  
Response Curve ◽  
Blood Clot ◽  
Morphological Characteristics ◽  
Fibrin Clot ◽  
Blood Clots ◽  
Isopeptide Bonds ◽  
Isopeptidase Activity ◽  
Stabilized Fibrin ◽  
Poisonous Animals

Leeches are amazing animals that can be classified as conditionally poisonous animals since the salivary cocktail they produce is injected directly into the victim, and its components have strictly defined biological purposes, such as preventing blood clot formation. Thrombolytic drugs are mainly aimed at treating newly formed blood clots. Aged clots are stabilized by a large number of isopeptide bonds that prevent the action of thrombolytics. These bonds are destroyed by destabilase, an enzyme of the leech’s salivary glands. Here, we conducted a pilot study to evaluate the feasibility and effectiveness of the use of destabilase in relation to blood clots formed during real pathological processes. We evaluated the isopeptidase activity of destabilase during the formation of a stabilized fibrin clot. We showed that destabilase does not affect the internal and external coagulation cascades. We calculated the dose–response curve and tested the ability of destabilase to destroy isopeptide bonds in natural blood clots. The effect of aged and fresh clots dissolving ability after treatment with destabilase coincided with the morphological characteristics of clots during surgery. Thus, recombinant destabilase can be considered as a potential drug for the treatment of aged clots, which are difficult to treat with known thrombolytics.

Fibrin and Fibrinogen Proteolysis Products: Comparison between Gel Filtration and SDS Polyacrylamide Electrophoresis Analysis

1977 ◽  
Vol 38 (02) ◽  
pp. 0524-0535 ◽  
Author(s):  
Norma Alkjaersig ◽  
Andrew Davies ◽  
Anthony Fletcher
Keyword(s):  
Molecular Weight ◽  
Analytical Methods ◽  
Gel Filtration ◽  
Molecular Size ◽  
The Other ◽  
Reaction Products ◽  
Human Fibrinogen ◽  
Polyacrylamide Electrophoresis ◽  
Large Molecular Weight ◽  
Stabilized Fibrin

SummaryThe proteolysis of purified human fibrinogen, stabilized and non-stabilized fibrin by plasmin were investigated by gel filtration analysis and SDS polyacrylamide electrophoresis of the reaction products. Plasmin proteolysis of fibrinogen followed the sequential steps previously reported and the two analytical methods yielded concordant results. Large molecular weight proteolysis products, of substantially greater molecular weight than native fibrinogen, were identified by gel filtration analysis following dissolution of stabilized and non-stabilized fibrin clots; with further incubation with plasmin, these proteolysis products gradually diminished in size. On the other hand, SDS polyacrylamide electrophoresis of these fibrin digests demonstrated that while non-stabilized fibrin yielded breakdown products similar in size to those obtained after proteolysis of fibrinogen, stabilized fibrin digests showed moieties of greater molecular size estimated to be of molecular weight 400,000 to 800,000. The final breakdown products of stabilized fibrin differed from those of fibrinogen and nonstabilized fibrin in that fragment D was present in the “double D” cross-linked form.

scholarly journals Study of the Normal Serum Activity Sensitizing Stabilized Fibrin to Urea Dispersion by Sephadex G. 200 Chromatography

1977 ◽  
Author(s):  
F. de Cataldo ◽  
F. Baudo ◽  
E. Mussini
Keyword(s):  
Ammonium Sulphate ◽  
Normal Serum ◽  
Final Concentration ◽  
Distilled Water ◽  
Platelet Poor Plasma ◽  
Serum Activity ◽  
Two Peaks ◽  
Phosphate Buffered Saline ◽  
Stabilized Fibrin ◽  
Second Peak

Clots from human normal native platelet-poor plasma are dispersed by the addition of urea at a final concentration of 2.5 M. The same clots, washed in buffered saline (pH 7.4), are not dispersed by urea, but are rendered susceptible to its dispersing action by prior incubation in normal undiluted plasma and serum or 33% ammonium sulphate fractions. The serum fraction was dissolved in and dialyzed against pH. 7.4 phosphate-buffered saline and analyzed by Sephadex G. 200 chromatography. Two peaks were obtained; the relative materials were dialyzed against pH. 7.4 phosphate-buffered distilled water, lyophilized and dissolved in saline. The activity sensitizing the stabilized fibrin to urea dispersion was recovered in the second peak material.

On Physiological Regulation of the Liquid State and Coagulation of Blood

1975 ◽  
Author(s):  
B. A. Kudrjashov
Keyword(s):  
Liquid State ◽  
Blood Stream ◽  
Threshold Concentration ◽  
Physiological Regulation ◽  
Fibrin Monomer ◽  
Enzymatic Lysis ◽  
Reflex Reaction ◽  
Heparin Complexes ◽  
Stabilized Fibrin

The fluidity of blood in a healthy organism is kept by means of reflex reaction initiated by thrombin appearing in blood stream in a threshold concentration. Heparin and activator of plasminogen are excreting in blood as a result of the reflex act. Heparin forms the complexes with fibrinogen, factors XIII, plasminogen, adrenalin and other factors. These compounds act as antiaggregating and antistabilizing agents on the fibrin monomer. They dissolve non-stabilized fibrin, even in the presence of EACA or antiplasmin. Complex plasmin-heparin carries out the enzymatic lysis of stabilized fibrin in the presence of the same inhibitors of fibrinolysis. The clearance of I131-thiombin in blood stream depends from the eomplexing of enzyme with heparin. Complex Thrombin-heparin is absorbed in liver. The accumulation of other heparin complexes take place in the lungs, what is important for quick lysis of fibrin monomer aggregates in the vessels of this organ.

Hereditary dysfibrinogenemia.

1985 ◽  
Vol 31 (4) ◽  
pp. 509-516 ◽  
Author(s):  
T C Bithell
Keyword(s):  
Wound Healing ◽  
Molecular Level ◽  
Single Amino Acid ◽  
Cross Linking ◽  
Coagulation Disorder ◽  
Amino Acid Substitutions ◽  
Biochemical Studies ◽  
Stabilized Fibrin ◽  
Fibrinogen Molecule ◽  
Functional Defects

Abstract Inherited qualitative abnormalities of fibrinogen have been documented in more than 100 families. These dysfibrinogenemias usually are clinically silent, but in some cases are associated with bleeding, thrombosis, or defective wound healing. Abnormalities of the fibrinogen molecule may impair any of the major steps involved in the conversion of fibrinogen into stabilized fibrin; i.e., cleavage of the fibrinopeptides by thrombin, polymerization, and cross-linking of fibrin. Biochemical studies of several abnormal fibrinogens have demonstrated that the functional defects are the result of single amino acid substitutions. The hereditary dysfibrinogenemias are the first coagulation disorder in which the pathophysiology has been elucidated on a molecular level. Studies of these "experiments of nature" have important implications in such diverse processes as wound healing and thrombosis.

Sign in / Sign up

Export Citation Format

Share Document