Epsilon-Aminocaproic Acid for Synovectomy in Haemophilic Patients

1972 ◽  
Vol 47 (3) ◽  
pp. 146-156 ◽  
Author(s):  
E. Storti ◽  
E. Ascari ◽  
R. Turpini ◽  
E. Molinari ◽  
G. Gamba ◽  
...  
Keyword(s):  
Aminocaproic Acid ◽  
Epsilon Aminocaproic Acid

Plasminogen Interactions with Immobilized Fibrinogen

1989 ◽  
Vol 62 (04) ◽  
pp. 1078-1082 ◽  
Author(s):  
Burt Adelman ◽  
Patricia Ouynn
Keyword(s):  
Immunosorbent Assay ◽  
Aminocaproic Acid ◽  
Enzyme Linked Immunosorbent Assay ◽  
Binding Regions ◽  
Dose Dependent Fashion ◽  
Epsilon Aminocaproic Acid ◽  
Dose Dependent

SummaryThis report describes the binding of plasminogen to fibrinogen adsorbed onto polystyrene wells. Binding was determined by enzyme linked immunosorbent assay. Both glu- and lys-plasminogen bound to immobilized fibrinogen in a dose-dependent fashion. However, more lys- than glu-plasminogen bound when equal concentrations of either were added to immobilized fibrinogen. Plasminogen binding was inhibited by epsilon aminocaproic acid indicating that binding was mediated via lysine-binding regions of plasminogen. Soluble fibrinogen added in excess of immobilized fibrinogen did not compete for plasminogen binding but fibrinogen fragments produced by plasmin digestion of fibrinogen did. Treatment of immobilized fibrinogen with thrombin caused a small but significant (p <0.01) increase in plasminogen binding. These studies demonstrate that immobilized fibrinogen binds both glu- and lys-plasminogen and that binding is mediated via lysine-binding regions. These interactions may facilitate plasminogen binding to fibrinogen adsorbed on to surfaces and to cells such as platelets which bind fibrinogen.

Determination of Epsilon Aminocaproic Acid Based on Charge Transfer Complexation with p-Nitrophenlol by Spectrophotometry

2020 ◽  
Vol 16 ◽  
Author(s):  
Sheng-Yun Li ◽  
Fang Tian
Keyword(s):  
Charge Transfer ◽  
Aminocaproic Acid ◽  
Concentration Limit ◽  
Official Method ◽  
Good Precision ◽  
Pharmaceutical Dosage Forms ◽  
Relative Standard ◽  
A Charge ◽  
Epsilon Aminocaproic Acid

: A spectrophotometry was investigated for the determination of epsilon aminocaproic acid (EACA) with p-nitrophenol (PNP). The method was based on a charge transfer (CT) complexation of this drug as n-electron donor with π-acceptor PNP. Experiment indicated that the CT complexation was carried out at room temperature for 10 minutes in dimethyl sulfoxide solvent. The spectrum obtained for EACA/PNP system showed the maximum absorption band at wavelength of 425 nm. The stoichiometry of the CT complex was found to be 1:1 ratio by Job’s method between the donor and the acceptor. Different variables affecting the complexation were carefully studied and optimized. At the optimum reaction conditions, Beer’s law was obeyed in a concentration limit of 1～6 µg mL-1. The relative standard deviation was less than 2.9%. The apparent molar absoptivity was determined to be 1.86×104 L mol-1cm-1 at 425 nm. The CT complexation was also confirmed by both FTIR and 1H NMR measurements. The thermodynamic properties and reaction mechanism of the CT complexation have been discussed. The developed method could be applied successfully for the determination of the studied compound in its pharmaceutical dosage forms with a good precision and accuracy compared to official method as revealed by t- and F-tests.

Pathological fibrinolytic states and their treatment with epsilon aminocaproic acid (EACA)

1966 ◽  
Vol 53 (1) ◽  
pp. 26-29 ◽  
Author(s):  
G. P. McNicol ◽  
M. K. Browne ◽  
Carolyn Bayley ◽  
A. S. Douglas
Keyword(s):  
Aminocaproic Acid ◽  
Epsilon Aminocaproic Acid

scholarly journals Management of Idiopathic Thrombocytopenic Purpura in Adult: A Review Article

2012 ◽  
Vol 2 (1) ◽  
pp. 24-28
Author(s):  
Mohammad Ferdous Ur Rahaman ◽  
Farzana Rahman ◽  
Mohammad Salman ◽  
Md. Abdul Kader ◽  
Md. Abdul Kalam Azad
Keyword(s):  
Clinical Presentation ◽  
Protein A ◽  
Spontaneous Remission ◽  
Aminocaproic Acid ◽  
Review Article ◽  
Bleeding Complications ◽  
Medical College ◽  
Chronic Disorder ◽  
Insidious Onset ◽  
Epsilon Aminocaproic Acid

Idiopathic thrombocytopenic purpiira (ITP), also known as primary immune or autoimmune thmmbocytopenic purpura, is a common cause of thrombocytopenia and bleeding complications in children and adults. It mav be confused with other causes of thrombocvtopenia and is treated with agents that varv in efjicacv, toxicity, and cost. Clinical presentation very in children and adult. In children, ITP is usually an acute, self-limited disorder that resolves spontaneously: in adults, it is typically a chronic disorder with a more insidious onset. In about one third of adults with ITP, the condition is persistent and relatively resistant to most treatments .Available evidence suggests that only about 5% of adults with chronic ITP have spontaneous remission. The principal therapeutic options for ITP include glucocorticoids, intravenous immunoglobulin and splenectomy. Other treatments have been used for refractory cases; these include intravenous anti-Rh (D), azathioprine, cyclophosphamide, danazol, vinca alkaloids, ascorbic acid, colchicine, interferon-alpha, combination chemotherapy, protein A, immunoadsorption, cyclosporine, epsilon-aminocaproic acid, plasma exchange, and accessory splenectomy. Journal of Shaheed Suhrawardy Medical College Vol 2No.1 June 2010 page 24-28 DOI: http://dx.doi.org/10.3329/jssmc.v2i1.12348

scholarly journals Systemic allergic dermatitis to epsilon-aminocaproic acid

2009 ◽  
Vol 61 (5) ◽  
pp. 303-304 ◽  
Author(s):  
Daniela Cunha ◽  
Rodrigo Carvalho ◽  
Raquel Santos ◽  
Jorge Cardoso
Keyword(s):  
Aminocaproic Acid ◽  
Allergic Dermatitis ◽  
Epsilon Aminocaproic Acid

scholarly journals Elective Synovectomy in Hemophilia

1977 ◽  
Author(s):  
Geni A. Bennetts ◽  
Marilyn G. Myers ◽  
Brian A. Ewald
Keyword(s):  
Joint Destruction ◽  
Aminocaproic Acid ◽  
Postoperative Management ◽  
Recurrent Bleeding ◽  
Joint Function ◽  
Radiographic Evidence ◽  
Manipulation Under Anesthesia ◽  
Epsilon Aminocaproic Acid ◽  
Initial Results

A total of twenty-one elective synovectomies and three repeat elective synovectomies, as stimulated by the work of Storti, et al., were performed on elbows, knees, and ankles of six patients with Classical Hemophilia (circulating antihemophiliac globulin factor VIII < 1%) from 1970-1976. Decision to perform surgery was based on recurrent bleeding into a joint, decrease in joint function, and radiographic evidence of joint destruction. The surgical protocol established included preoperative therapy with commercial Antihemophiliac Globulin Concentrate (AHG) and epsilon aminocaproic acid. Surgical synovectomy was followed by postoperative management which included parenteral therapy with AHG and epsilon aminocaproic acid, joint drainage and, in addition, interarticular epsilon aminocaproic acid and antibiotics with mobilization. When indicated, manipulation under anesthesia combined with a regimen of physical therapy was carried out. Initial results were encouraging, but enthusiasm after up to six years follow-up has been tempered by recurrence of hemarthroses and further radiographic deterioration in several of the synovectomized joints. This has necessitated the three aforementioned repeat synovectomies.

Cleavage of human von Willebrand factor by platelet calcium-activated protease

Blood ◽  
1985 ◽  
Vol 65 (2) ◽  
pp. 352-356 ◽  
Author(s):  
TJ Kunicki ◽  
RR Montgomery ◽  
J Schullek
Keyword(s):  
Von Willebrand Factor ◽  
Sodium Dodecylsulfate ◽  
Apparent Molecular Weight ◽  
Aminocaproic Acid ◽  
Crossed Immunoelectrophoresis ◽  
Nonionic Detergent ◽  
Epsilon Aminocaproic Acid ◽  
Triton X ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract In human platelet lysates prepared by addition of nonionic detergent (Triton X-100) or by sonication, the multimer composition and electrophoretic mobility of platelet von Willebrand factor (vWF) were consistently modified under conditions that would favor activation of the endogenous calcium-activated, sulfhydryl-dependent neutral protease (CAP). By sodium dodecylsulfate-agarose gel electrophoresis, native platelet vWF contained some multimers that were larger than those characteristic of plasma vWF. Modified platelet vWF contained a multimer population equivalent to or smaller than that of plasma vWF plus an additional fast-migrating band. In crossed immunoelectrophoresis (CIE), modified platelet vWF was characterized by a more anodic distribution and the appearance of a distinct, cross- reactive, anodic component previously designated VIIIR:Ag fragment. In the presence of calcium, radiolabeled purified plasma vWF was also degraded by the protease in question, with a decrease in the apparent molecular weight of the reduced monomer from 230,000 to 205,000. The VIIR:Ag fragment isolated from the same degraded plasma vWF by preparative CIE was shown to be composed of an identical mol wt 205,000 subunit. Because cleavage of plasma or platelet vWF was inhibited by prior addition of leupeptin, EDTA, ethylene glycol bis (beta-aminoethyl ether)-N, N, N′, N′-tetraacetic acid (EGTA), or N-ethylmaleimide (agents known to inhibit platelet CAP) but was unaffected by numerous other protease inhibitors, including soybean trypsin inhibitor, benzamidine, hirudin, phenylmethylsulfonyl fluoride, aprotonin, or epsilon-aminocaproic acid (none of which inhibits platelet CAP), we conclude that proteolysis of vWF observed in this study is a direct effect of CAP and is not mediated by way of secondary proteases.

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