Activation of the Catalytic Activity of Thrombin for Fibrin Formation by Ultrasound

Rare-earth phosphates are of particular interest because of their catalytic properties associated with the hydrolysis of many aromatic chlorides in the petroleum industry. Lanthanum phosphates (LaPO4) which have been doped with small amounts of copper have shown increased catalytic activity (1). However the physical and chemical characteristics of the samples leading to good catalytic activity are not known.Many catalysts are amorphous and thus do not easily lend themselves to methods of investigation which would include electron microscopy. However, the LaPO4, crystals are quite suitable samples for high resolution techniques.The samples used were obtained from William L. Kehl of Gulf Research and Development Company. The electron microscopy was carried out on a JEOL JEM-100B which had been modified for high resolution microscopy (2). Standard high resolution techniques were employed. Three different sample types were observed: 669A-1-5-7 (poor catalyst), H-L-2 (good catalyst) and 27-011 (good catalyst).

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The design and catalytic performance of molybdenum active sites on an MCM-41 framework for the aerobic oxidation of 5-hydroxymethylfurfural to 2,5-diformylfuran

Catalysis Science & Technology ◽

10.1039/c8cy02291g ◽

2019 ◽

Vol 9 (3) ◽

pp. 811-821 ◽

Cited By ~ 7

Author(s):

Zhao-Meng Wang ◽

Li-Juan Liu ◽

Bo Xiang ◽

Yue Wang ◽

Ya-Jing Lyu ◽

...

Keyword(s):

Catalytic Activity ◽

Active Sites ◽

Aerobic Oxidation ◽

Catalytic Performance ◽

Mcm 41

The catalytic activity decreases as –(SiO)3Mo(OH)(O) > –(SiO)2Mo(O)2 > –(O)4–MoO.

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Relationship Between Fibrinopeptide A and Fibrinogen/Fibrin Fragment E in Thromboembolism, DIC and Various Non-Thromboembolic Diseases

Thrombosis and Haemostasis ◽

10.1055/s-0038-1645965 ◽

1987 ◽

Vol 58 (02) ◽

pp. 758-763 ◽

Cited By ~ 11

Author(s):

G Mombelli ◽

R Monotti ◽

A Haeberli ◽

P W Straub

Keyword(s):

Myocardial Infarction ◽

Acute Myocardial Infarction ◽

Liver Cirrhosis ◽

Healthy Subjects ◽

Vascular Diseases ◽

Fibrinopeptide A ◽

Normal Range ◽

Collagen Vascular Diseases ◽

Intravascular Coagulation ◽

Fibrin Formation

SummaryIncreased fibrinopeptide A (FPA) levels have been reported in various non-thrombotic disorders, including cancer, acute myocardial infarction, liver cirrhosis and collagen vascular diseases. To investigate the significance of these findings, the present study combined the radioimmunoassay of FPA with that of fibrinogen/fibrin degradation fragment E (FgE) in the aforementioned disorders and compared the results with those observed in healthy subjects as well as in patients with thromboembolism and overt disseminated intravascular coagulation (DIC). Mean FPA and FgE in malignancy were 6.3 and 305 ng/ml, in myocardial infarction 5.6 and 98 ng/ml, in liver cirrhosis 2.7 and 132 ng/ml and in collagen vascular diseases 5.6 and 142 ng/ml. All these values were significantly higher than in healthy controls (mean FPA 1.6 ng/ml, mean FgE 49 ng/ml) but significantly lower than in thromboembolism (mean FPA 10.7 ng/ml, mean FgE 639 ng/ ml) and DIC (mean FPA 22.0 ng/ml, mean FgE 1041 ng/ml). The overall correlation between FPA and FgE was highly significant. Elowever, different disorders showed peculiar patterns in FPA, FgE and fibrinogen levels. In malignancy, a definite increase of FPA, FgE and plasma fibrinogen levels was observed. This finding probably indicates a compensated state of (intra- or extravascular) fibrin formation and lysis. Acute myocardial infarction was characterized by a high FPA to FgE ratio, which is interpreted to reflect acute thrombin generation and fibrin formation. FPA in cirrhosis was only marginally elevated with most single values within the normal range, indicating that intravascular coagulation was infrequent and unimportant in quantitative terms.

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Fibrin Formation: The Role of the Fibrinogen-Fibrin Monomer Complex

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648007 ◽

1976 ◽

Vol 36 (01) ◽

pp. 037-048 ◽

Cited By ~ 49

Author(s):

Eric P. Brass ◽

Walter B. Forman ◽

Robert V. Edwards ◽

Olgierd Lindan

Keyword(s):

Particle Size ◽

Induction Period ◽

Fibrin Clot ◽

Clot Formation ◽

Appreciable Amount ◽

Buffer System ◽

Homeostatic Mechanism ◽

Fibrin Formation ◽

Fibrin Monomer

SummaryThe process of fibrin formation using highly purified fibrinogen and thrombin was studied using laser fluctuation spectroscopy, a method that rapidly determines particle size in a solution. Two periods in fibrin clot formation were noted: an induction period during which no fibrin polymerization occurred and a period of rapid increase in particle size. Direct measurement of fibrin monomer polymerization and fibrinopeptide release showed no evidence of an induction period. These observations were best explained by a kinetic model for fibrin clot formation incorporating a reversible fibrinogen-fibrin monomer complex. In this model, the complex serves as a buffer system during the earliest phase of fibrin formation. This prevents the accumulation of free polymerizable fibrin monomer until an appreciable amount of fibrinogen has reacted with thrombin, at which point the fibrin monomer level rises rapidly and polymerization proceeds. Clinically, the complex may be a homeostatic mechanism preventing pathological clotting during periods of elevated fibrinogen.

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Prolonged Expression of Procoagulant Activity of Human Platelets Degranulated by Thrombin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649855 ◽

1995 ◽

Vol 74 (03) ◽

pp. 958-961 ◽

Cited By ~ 6

Author(s):

Raelene L Kinlough-Rathbone ◽

Dennis W Perry

Keyword(s):

Catalytic Activity ◽

Thrombus Formation ◽

Annexin V ◽

Human Platelets ◽

Procoagulant Activity ◽

Prothrombinase Complex ◽

Arterial Thrombus ◽

Flowing Blood

SummaryPlatelets are exposed to thrombin when they take part in arterial thrombus formation, and they may return to the circulation when they are freed by fibrinolysis and dislodged by flowing blood. Thrombin causes the expression of procoagulant activity on platelets, and if this activity persists, the recirculating platelets may contribute to subsequent thrombosis. We have developed techniques to degranulate human platelets by treatment with thrombin, and recover them as single, discrete platelets that aggregate in response to both weak and strong agonists. In the present study we examined the duration of procoagulant activity on the surface of thrombin-degranulated platelets by two methods: a prothrombinase assay, and the binding of 125I-labeled annexin. Control platelets generated 0.9 ± 0.4 U thrombin per 107 platelets in 15 min. Suspensions of thrombin-degranulated platelets formed 5.4 ± 0.1 U thrombin per 107 platelets in this time. Binding of 125I-annexin V was also greater with thrombin-treated platelets than with control platelets (controls: 1.7 ±0.1 ng annexin/107 platelets; thrombin-degranulated platelets: 6.8 ± 0.2 ng annexin/107 platelets). With thrombin-degranulated platelets, increased procoagulant activity and annexin binding persisted for at least 4 h after degranulation and resuspension, indicating that the catalytic activity for the prothrombinase complex is not reversed during this time. These platelets maintained their ability to aggregate for 4 h, even in response to the weak agonist, ADP. Thus, platelets that have taken part in thrombus formation and returned to the circulation may contribute to the promotion of further thrombotic events because of the persistence of procoagulant activity on their surface.

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A 3.5-Second Phenomenon in Haemostasis

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649086 ◽

1973 ◽

Vol 30 (02) ◽

pp. 363-370

Author(s):

D Thilo ◽

E Böhm

Keyword(s):

Bleeding Time ◽

Rat Skin ◽

Fibrin Formation ◽

Bleeding Area ◽

Platelet Thrombus ◽

Platelet Aggregates ◽

Primary Platelet ◽

System Mechanism

SummaryExperiments with injury of the abdominal rat skin were carried out to examine the haemostatic system mechanism in vivo after zero to 30 seconds bleeding time. In the bleeding area only a few platelet aggregates could be found with no primary platelet thrombus. After 3.5 second bleeding time the first fibrin strands have been observed at the site of injury. The hypothesis is put forward that there is a very fast reacting haemostatic mechanism which results in the fibrin formation already at 3.5 seconds.

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The Intravascular Generation of Fibrinogen Derivatives and the Blood Vessel Wall in Venous Thrombosis and Disseminated Intravascular Coagulation

Thrombosis and Haemostasis ◽

10.1055/s-0038-1651902 ◽

1977 ◽

Vol 38 (04) ◽

pp. 0831-0849 ◽

Cited By ~ 1

Author(s):

Gwendolyn J. Stewart

Keyword(s):

Blood Vessel ◽

Venous Thrombosis ◽

Vessel Wall ◽

Fluid Phase ◽

Primary Site ◽

Blood Vessel Wall ◽

Fibrin Deposition ◽

Tissue Destruction ◽

Fibrin Formation ◽

Rich Material

SummaryBoth deep venous thrombosis and DIC are intermediate mechanisms of disease – both are a consequence of the deposition of fibrin-rich material in blood vessels some distance from the primary site of tissue destruction. The great difference in the sites of fibrin deposition may depend on the extent and site of activation of the clotting mechanism. DIC likely occurs in the fluid phase of the blood as a consequence of massive fibrin formation while thrombosis results from limited fibrin formation at the interface between blood and vessel wall. Leukocytes may be essential for attaching thrombi to the vessel wall in many places.

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The Anticoagulant Effect of Heparinoid Org 10172 During Haemodialysis: An Objective Assessment

Thrombosis and Haemostasis ◽

10.1055/s-0038-1661535 ◽

1986 ◽

Vol 55 (02) ◽

pp. 271-275 ◽

Cited By ~ 22

Author(s):

Helen Ireland ◽

D A Lane ◽

Angela Flynn ◽

E Anastassiades ◽

J R Curtis

Keyword(s):

Renal Failure ◽

Bolus Dose ◽

Bolus Injection ◽

Objective Assessment ◽

Factor Xa ◽

Fibrin Clot ◽

Natural Origin ◽

Fibrin Formation ◽

Single Bolus Injection

SummaryThe heparinoid of natural origin Org 10172 has anti-factor Xa activity but minimal anti-thrombin activity, and little effect upon broad spectrum assays such as the KCCT in vitro. Its anticoagulant effects have been compared to those of commercial heparin in 7 patients undergoing haemodialysis for chronic renal failure. Commercial heparin was administered in a dose (5,000 iu bolus + 1,500 iu/hour continuous iv infusion) previously shown to inhibit fibrin formation during haemodialysis. This produced mean anti-factor Xa levels in plasma between 0.7-1.0 iu/ml and largely suppressed fibrin formation for 5 h dialysis measured as mean FPA levels in plasma. Administration of Org 10172 as a bolus of 1,350 anti-factor Xa u or 2,000-2,400 anti-factor Xa u produced plasma anti-factor Xa levels of less than 0.5 u/ml and allowed fibrin clot and FPA generation during dialysis. Org 10172 administered as a bolus dose of 4,000-4,800 anti-factor Xa u produced mean anti-factor Xa levels of greater than 0.5 u/ml, allowed dialysis of 6 patients for 5 h and appreciably suppressed FPA generation during dialysis, with little effect on the KCCT.It is concluded that the anti-factor Xa activity of Org 10172 may reflect its ability to inhibit fibrin during dialysis and that single bolus injection of Org 10172 may be a useful alternative method of achieving anticoagulation.

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Enhanced catalytic activity of low-Pt content nanocatalysts supported on hollow carbon spheres for the ORR in alkaline media

MRS Advances ◽

10.1557/adv.2020.370 ◽

2020 ◽

Vol 5 (57-58) ◽

pp. 2961-2972

Author(s):

P.C. Meléndez-González ◽

E. Garza-Duran ◽

J.C. Martínez-Loyola ◽

P. Quintana-Owen ◽

I.L. Alonso-Lemus ◽

...

Keyword(s):

Catalytic Activity ◽

Anion Exchange ◽

Average Particle Size ◽

Synthesis Method ◽

Alkaline Media ◽

High Catalytic Activity ◽

Average Particle ◽

Carbon Spheres ◽

Hollow Carbon ◽

Hollow Carbon Spheres

In this work, low-Pt content nanocatalysts (≈ 5 wt. %) supported on Hollow Carbon Spheres (HCS) were synthesized by two routes: i) colloidal conventional polyol, and ii) surfactant-free Bromide Anion Exchange (BAE). The nanocatalysts were labelled as Pt/HCS-P and Pt/HCS-B for polyol and BAE, respectively. The physicochemical characterization of the nanocatalysts showed that by following both methods, a good control of chemical composition was achieved, obtaining in addition well dispersed nanoparticles of less than 3 nm TEM average particle size (d) on the HCS. Pt/HCS-B contained more Pt0 species than Pt/HCS-P, an effect of the synthesis method. In addition, the structure of the HCS remains more ordered after BAE synthesis, compared to polyol. Regarding the catalytic activity for the Oxygen Reduction Reaction (ORR) in 0.5 M KOH, Pt/HCS-P and Pt/HCS-B showed a similar performance in terms of current density (j) at 0.9 V vs. RHE than the benchmark commercial 20 wt. % Pt/C. However, Pt/HCS-P and Pt/HCS-B demonstrated a 6 and 5-fold increase in mass catalytic activity compared to Pt/C, respectively. A positive effect of the high specific surface area of the HCS and its interactions with metal nanoparticles and electrolyte, which promoted the mass transfer, increased the performance of Pt/HCS-P and Pt/HCS-B. The high catalytic activity showed by Pt/HCS-B and Pt/HCS-P for the ORR, even with a low-Pt content, make them promising cathode nanocatalysts for Anion Exchange Membrane Fuel Cells (AEMFC).

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