The effect of fibrinogen degradation products and some lysine analogues on the dissociation of plasmin(ogen) - fibrin complexes

Cederholm‐Williams, S.A.; Swain, Ayusman

doi:10.1016/0049-3848(79)90214-7

Cited by 21 publications

(3 citation statements)

References 11 publications

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“…Our result that there are two sequentially nonidentical regions of fibrin(ogen) that carry plasminogen-binding site is at variance with the conclusion of Cederholm- Williams & Swain (1979) that only the E domain has a plasminogenbinding site. These authors studied the effect of fragments D and E on the incorporation of Lys-plasminogen into fibrin clots and found that whereas fragment E could inhibit binding, fragment D was without effect.…”

Section: Discussioncontrasting

confidence: 82%

Location of plasminogen-binding sites in human fibrin(ogen)

Váradi¹,

Patthy²

1983

Biochemistry

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Affinity chromatography of various fibrinogen and fibrin fragments on Lys-plasminogen-Sepharose was used to localize the plasminogen-binding sites in human fibrin(ogen). The fragments studied in the present investigation were derived from the central (E) and the terminal (D) globular domains of fibrinogen and fibrin. Our results showed that these two different, sequentially nonidentical domains of fibrin(ogen) both carry plasminogen-binding sites. Competitive affinity chromatography of fragment D1 and fragments derived from it by proteolytic modification of its D gamma-chain revealed that this modification causes an 11-fold increase of the association constant of the interaction with Lys-plasminogen-Sepharose. This suggests that the carboxy-terminal region of the D gamma-chain is involved in controlling the plasminogen-binding site of the D domain. In contrast with its fragments, intact fibrinogen is not retained by Lys-plasminogen-Sepharose, indicating that the plasminogen-binding sites present in the constituent E and D domains are not fully functional in the parent molecule. It seems possible that the plasminogen-binding sites are present but hidden in fibrinogen and proteolytic dissection of the molecule uncovers these sites in E and D fragments by removing peptides masking the plasminogen-binding regions.

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Section: Discussioncontrasting

confidence: 82%

Location of plasminogen-binding sites in human fibrin(ogen)

Váradi¹,

Patthy²

1983

Biochemistry

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“…In this study, we have measured the affinity of native plasminogen and partly degraded plasminogen for fibrinogen under equilibrium conditions. The affinity for lysine analogues in plasminogen and its fragments (kringles 1-4 and miniplasminogen) has been investigated extensively by using insoluble interacting components such as fibrin or lysine-linked solid matrices (Cederholm-Williams & Swain, 1979;Suenson & Thorsen, 1981;Thorsen et al, 1981;Lucas et al, 1983;Varadi & Patthy, 1983). However, very little has been reported on the binding properties of plasminogen to fibrinogen, which are the physiological constituents of plasma.…”

Section: Discussionmentioning

confidence: 99%

Cooperative association of plasminogen with fibrinogen

Lewis¹,

Carmassi²,

Chung³

1984

Biochemistry

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We have examined the association of both Glu- and Lys-plasminogen to fibrinogen by ultracentrifugal sedimentation equilibrium in neutral isotonic buffer in the presence of aprotinin. The fibrinogen and plasminogens, which were homogenous, did not exhibit any self-association. In each association study, five different molar ratios of plasminogen to fibrinogen were examined. The data were analyzed by mathematical modeling using nonlinear least-squares curve fitting. Analyses of molecular species present showed that up to 4 mol of either Glu- or Lys-plasminogen was associated with each mol of fibrinogen. For the binding of Glu-plasminogen, the values of the successive changes of the standard free energy of association were found to be -5.48, -7.73, -8.88, and -11.41 kcal/mol (Ka = 2.16 X 10(4), 1.32 X 10(6), 1.06 X 10(7), and 1.08 X 10(9) M-1). For the experimental conditions used here, the association of Lys-plasminogen appears to be described by virtually the same fitting parameters. The very marked cooperativity of association found here would appear to imply that there are significant alterations of the structure of fibrinogen as a result of each successive molecule of plasminogen bound.

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“…) used in a broad spectrum of peri-and postoperative interventions and bleeding disorders 1,2 . The administration of TRA is associated with a reduction in bleeding due to its inhibitory effect on clot breakdown (fibrinolysis).…”

mentioning

confidence: 99%

Spectrophotometric Methods for Determination of Tranexamic Acid and Etamsylate in Pure Form and Pharmaceutical Formulation

Frag¹,

Sedeek²

2015

Insight Pharmaceutical Sciences

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Background: Tranexamic acid and etamsylate drugs belong to a group of antifibrinolytics. Tranexamic Acid (TRA) is the most potent antifibrinolytic lysine analogue used in a broad spectrum of peri-and postoperative interventions and bleeding disorders. The administration of TRA is associated with a reduction in bleeding due to its inhibitory effect on clot breakdown (fibrinolysis). Etamsylate (ESL) is a haemostatic agent that appears to maintain the stability of the capillary wall and correct abnormal platelet adhesion. It is given for the prophylaxis and control of haemorrhages from small blood vessels. Objective: Two simple and sensitive spectrophotometric methods are described for the determination of tranexamic acid (TRA) and etamsylate (ESL) drugs in pure form and pharmaceutical preparations. Materials and Methods Method (A) is used for the determination of TRA and based on condensation reaction of the primary amino group of TRA with salicylaldehyde reagent (SA) (Schiff base formation) producing a yellow coloured product which is measured spectrophotometrically at 400 nm. Method (B) is utilized for the determination of ESL and based on the oxidation-reduction reaction of ESL using iodic acid (HIO 3). The liberated iodine was extracted in chloroform and the absorbance of the red coloured product is measured spectrophotometrically at 510 nm. For method A and B, different variables affecting the reactions were studied and optimized. Results: Under the optimum conditions, linear relationships with good correlation coefficients 0.9989 and 0.9959 were found between the absorbance and the concentration of the drug in the range from 5 to 500 and 2.5 to 275 μg mLG 1 for ESL and TRA drugs, respectively. The limit of detection (μg mLG 1), limit of quantification (μg mLG 1) and molar absorptivity (L molG 1 cmG 1) values were found to be 1.442, 4.80 and 5.39×10 2 for TRA drug and 2.20, 7.25 and 3.0×10 2 for ESL drug, respectively. Conclusion: The method was applied for determination of the investigated drugs in tablets. The method was validated and can be suggested for routine analysis of both drugs.

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The effect of fibrinogen degradation products and some lysine analogues on the dissociation of plasmin(ogen) - fibrin complexes

Cited by 21 publications

References 11 publications

Location of plasminogen-binding sites in human fibrin(ogen)

Location of plasminogen-binding sites in human fibrin(ogen)

Cooperative association of plasminogen with fibrinogen

Spectrophotometric Methods for Determination of Tranexamic Acid and Etamsylate in Pure Form and Pharmaceutical Formulation

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