Academic literature on the topic 'Anti-thrombin'

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Journal articles on the topic "Anti-thrombin"

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Sosolik, Randy C., Karl S. Theil, and John T. Brandt. "Anti-Bovine Thrombin Antibody." Laboratory Medicine 27, no. 10 (1996): 651–54. http://dx.doi.org/10.1093/labmed/27.10.651.

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EVINGTON, JOHN R. N., PETER A. FELDMAN, MOLLIE LUSCOMBE, and J. JOHN HOLBROOK. "Fluorescence polarization studies of the thrombin/anti-thrombin reactions." Biochemical Society Transactions 13, no. 4 (1985): 773–74. http://dx.doi.org/10.1042/bst0130773a.

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Proulle, Valerie, Celine Desconclois, Cecile Lavenu-Bombled, Cecile Goujard, Anish V. Sharda, and Ali G. Turhan. "Severe Acquired Bleeding Tendency Secondary To An Anti-Thrombin Antibody In a Patient With Monoclonal Gammapathy Of Unknown Significance: Direct In Vivo evidence." Blood 122, no. 21 (2013): 1111. http://dx.doi.org/10.1182/blood.v122.21.1111.1111.

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Abstract Introduction Anti-thrombin antibodies are a rare cause of acquired bleeding disorder. We report a case of a patient with a monoclonal gammapathy of unknown significance (MGUS) referred to us for an acquired bleeding tendency. We found that he had an isolated anti-thrombin antibody and showed that this antibody inhibit platelet accumulation and fibrin generation in vivo in a mouse model of arterial thrombus formation. Patient A 40-year-old man with no personal or familial history of bleeding was referred to us for multiple bleeding episodes (rectal bleeding, hematoma) for 18 years. He
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Norton, KJ, RM Scarborough, JL Kutok, MA Escobedo, L. Nannizzi, and BS Coller. "Immunologic analysis of the cloned platelet thrombin receptor activation mechanism: evidence supporting receptor cleavage, release of the N-terminal peptide, and insertion of the tethered ligand into a protected environment." Blood 82, no. 7 (1993): 2125–36. http://dx.doi.org/10.1182/blood.v82.7.2125.2125.

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Abstract The recently cloned functional thrombin receptor is thought to be activated by thrombin cleavage of the bond between R41 and S42, followed by the insertion of the new N-terminal region (“tethered ligand”) into an unknown site in the receptor. Antibodies to peptides at or near the cleavage site have been reported to inhibit thrombin- induced platelet activation to varying extents, but the precise mechanism(s) of their inhibition is unknown. We have produced: (1) a polyclonal antibody in rabbits to a peptide containing amino acids 34 to 52 (anti-TR34–52); enzyme-linked immunosorbent ass
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Norton, KJ, RM Scarborough, JL Kutok, MA Escobedo, L. Nannizzi, and BS Coller. "Immunologic analysis of the cloned platelet thrombin receptor activation mechanism: evidence supporting receptor cleavage, release of the N-terminal peptide, and insertion of the tethered ligand into a protected environment." Blood 82, no. 7 (1993): 2125–36. http://dx.doi.org/10.1182/blood.v82.7.2125.bloodjournal8272125.

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The recently cloned functional thrombin receptor is thought to be activated by thrombin cleavage of the bond between R41 and S42, followed by the insertion of the new N-terminal region (“tethered ligand”) into an unknown site in the receptor. Antibodies to peptides at or near the cleavage site have been reported to inhibit thrombin- induced platelet activation to varying extents, but the precise mechanism(s) of their inhibition is unknown. We have produced: (1) a polyclonal antibody in rabbits to a peptide containing amino acids 34 to 52 (anti-TR34–52); enzyme-linked immunosorbent assays (ELIS
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Kimura, M., T. T. Andersen, J. W. Fenton, W. F. Bahou, and A. Aviv. "Plasmin-platelet interaction involves cleavage of functional thrombin receptor." American Journal of Physiology-Cell Physiology 271, no. 1 (1996): C54—C60. http://dx.doi.org/10.1152/ajpcell.1996.271.1.c54.

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We tested the hypothesis that the inhibition of thrombin-induced platelet activation by plasmin is mediated via the enzymatic action of plasmin on the functional thrombin receptor. We monitored the binding of the anti-thrombin receptor antibody [anti-TR-(34-46)] to platelets; this binding is sensitive to the cleavage of the thrombin receptor at amino acid residues Arg-41 to Ser-42. Plasmin inhibited anti-TR-(34-46) binding in dose- and time-dependent manners. The inactive synthetic peptide with the amino acid sequence 40-55 of the thrombin receptor (D-FPRSFLLRNPNDKYEPF) was similarly cleaved b
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Billoir, Paul, Thomas Elie, Jerrold H. Levy, et al. "Anticoagulation Monitoring with Activated Partial ThromboPlastin Time and Anti-Xa Activity in Intensive Care Unit Patients: Interest of Thrombin Generation Assay." International Journal of Molecular Sciences 23, no. 19 (2022): 11219. http://dx.doi.org/10.3390/ijms231911219.

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Current guidelines recommend monitoring the anticoagulant effect of unfractionated heparin (UFH) by measuring anti-Xa activity rather than activated partial thromboplastin time (aPTT) in intensive care unit (ICU) patients. The primary objective of this study was to evaluate the correlation of aPTT, anti-Xa activity, and thrombin generation in UFH-treated ICU patients. A prospective observational pilot study was conducted in adult surgical ICU patients treated with UFH. aPTT and anti-Xa activity were monitored daily. The therapeutic target was aPTT between 50 s and 84 s, and/or anti-Xa between
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Dolor, MC, and M. Kastetter. "Anti-D in human thrombin." Transfusion 26, no. 2 (1986): 215. http://dx.doi.org/10.1046/j.1537-2995.1986.26286152922.x.

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Leclerc, J. R., W. Geerts, A. Panju, P. Nguyen, and J. Hirsh. "Management of anti-thrombin III deficiency during pregnancy without administration of anti-thrombin III." Thrombosis Research 41, no. 4 (1986): 567–73. http://dx.doi.org/10.1016/0049-3848(86)91702-0.

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Brisson, Christine, Gisèle Archipoff, Marie-Louise Hartmann, et al. "Antibodies to Thrombomodulin Induce Receptor-Mediated Endocytosis in Human Saphenous Vein Endothelial Cells." Thrombosis and Haemostasis 68, no. 06 (1992): 737–43. http://dx.doi.org/10.1055/s-0038-1646353.

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SummaryThe membrane glycoprotein thrombomodulin (TM) is an essential endothelial cell (EC) cofactor, which forms a 1:1 stoichiometric complex with thrombin. Binding of thrombin to the high affinity TM receptor transforms its procoagulant activity into an anticoagulant potential, by activating protein C. The fate of TM in the presence of thrombin is still unclear: some authors claim that the thrombin-TM complex is internalized in EC, while others find this complex to be stable for at least 2 h at 37° C on the EC surface. In the present study, we investigated the interactions of thrombin and Fab
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Dissertations / Theses on the topic "Anti-thrombin"

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Sidhu, Preetpal. "Designing Allosteric Inhibitors of Thrombin." VCU Scholars Compass, 2011. http://scholarscompass.vcu.edu/etd/295.

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Thrombin is a key enzyme of the coagulation cascade exhibiting important roles in both pro-coagulation and anti-coagulation processes. Most clinically used anticoagulant drugs, including polymeric heparin, warfarin, hirudin, argatroban and the recently approved dabigatran, aim to reduce thrombin activity. There are several binding domains on thrombin including the active site, anion-binding exosites I and II, and the sodium binding site. We hypothesized that thrombin may be better regulated through an allosteric process mediated by small molecules binding to either exosite I or II. An appropri
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Bhavaraju, Kamala. "MOLECULAR PHYSIOLOGY OF THROMBOXANE A2 GENERATION IN PLATELETS." Diss., Temple University Libraries, 2010. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/92746.

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Molecular and Cellular Physiology<br>Ph.D.<br>Cardiovascular diseases are a major cause of mortality and morbidity in the developed countries. Anti-platelet therapy is a cornerstone treatment for patients with cardiovascular diseases. Patients are routinely managed with a combination therapy consisting of aspirin and clopidogrel. Aspirin inhibits cyclooxygenase 1 (COX 1) a crucial intermediate enzyme involved in thromboxane biosynthesis. Clopidogrel on the other hand antagonizes ADP receptor P2Y12. ADP is a weak platelet agonist stored in platelet dense granules and is released upon platelet a
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Guéret, Pierre. "Développement clinique de l'EP217609 et de son antidote l'avidine." Thesis, Brest, 2017. http://www.theses.fr/2017BRES0130.

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Les pentasaccharides sont des inhibiteurs indirects du facteur Xa ayant des profils pharmacocinétiques très prédictibles. En raison de la liaison de forte affinité des pentasaccharides à l'antithrombine, cette pharmacocinétique peut être prédite mais aussi transférée à d'autres molécules qui leur sont liées de manière covalente. L'EP42675 combine dans une seule molécule, une antithrombine directe réversible peptidomimétique (analogue de l'α-NAPAP), et un pentasaccharide inhibiteur indirect du facteur Xa antithrombine dépendant (analogue du fondaparinux). L'EP217609 est le dérivé biotinylé de l
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Daniel, Camille. "Biopuce à aptamères anti-thrombine : exploration d'une technique alternative de détection." Phd thesis, Université de Grenoble, 2013. http://tel.archives-ouvertes.fr/tel-00954086.

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Du fait de leur haute stabilité et bas coût de production, les aptamères suscitent un intérêt croissant, depuis près de 20 ans, dans le design de biocapteurs en tant qu'élément de reconnaissance idéal. Le but de ce travail de thèse est de démontrer l'intérêt et la pertinence d'un outil tel qu'une biopuce à aptamères, associant les avantages des sondes aptamères à ceux d'une détection par SPRi (Surface Plasmon Resonance imaging), permettant une détection sans marquage et en temps réel d'interactions moléculaires. Dans ce but, deux aptamères anti-thrombine (APT1 = 5′- GGT-TGG-TGT-GGT-TGG -3′ et
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Chelle, Pierre. "Vers une définition patient-spécifique du taux cible de facteur anti-hémophilique à partir de la génération de thrombine : Apports des approches expérimentales et des modèles dynamiques de la cascade de la coagulation." Thesis, Lyon, 2017. http://www.theses.fr/2017LYSEM014/document.

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L’hémophilie est une maladie génétique se traduisant par la déficience des facteurs VIII et IX de la coagulation et conduisant à une tendance hémorragique. L’intensité des traitements substitutifs en facteur VIII et IX est définie essentiellement sur le taux basal du facteur déficitaire et non pas sur la capacité propre à chaque patient à générer de la thrombine qui est l’enzyme clé dans la formation du caillot de fibrine. Le test de génération de thrombine pourrait être utilisé pour permettre une individualisation du traitement anti-hémophilique. En effet, le taux de facteur VIII ou IX nécess
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Said, Rose. "Caractérisation des propriétés pro- et anti-coagulantes associées aux cellules musculaires lisses vasculaires." Thesis, Université de Lorraine, 2012. http://www.theses.fr/2012LORR0004/document.

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L'objectif principal de ce travail était de comparer l'implication (i) de cellules vasculaires, cellules musculaires lisses vasculaires (CML) et cellules endothéliales (CE), ou des cellules circulantes, les plaquettes, et (ii) des microparticules (MP) issues de ces différentes cellules dans la génération de la thrombine mais également dans son inhibition par les systèmes anticoagulants de la protéine C activée (PCa) et de l'inhibiteur de la voie du facteur tissulaire (TFPI), et d'identifier les mécanismes et les déterminants responsables des différences observées entre ces supports cellulaires
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Siao, Yi-di, and 蕭伊迪. "Preparation of a DNA aptamer-Pt Complex and its Use in the Colorimetric Sensing of Thrombin and Anti thrombin Antibodies." Thesis, 2008. http://ndltd.ncl.edu.tw/handle/26718719430702430857.

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碩士<br>國立中央大學<br>化學工程與材料工程研究所<br>96<br>DNA aptamers carrying Pt nanoparticles were prepared by the reaction of DNA aptamers (without functionalization with biotin, thiol or other reactive groups) with K2(PtCl4) in solution at 60-90 °C. The DNA-Pt complexes possessed peroxidase enzymatic activity while retaining the specific binding ability of the aptamers. The enzymatic reaction of these complexes obeyed Michaelis-Menten kinetics. Km for the DNA-Pt complex was found to be on the same order as Km for hemin and hemin-DNA complex, but two orders of magnitude higher than that of horseradish peroxid
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Yang, Chi-Wei, and 楊騏瑋. "Study on the Anti-thrombin, Anti-platelet Aggregation, and Antiviral Activity of Oversulfated Marine Algal Oligosaccharides and Its Adsorption Performance with Caco-2 Cell." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/13272239951691042027.

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碩士<br>國立臺灣海洋大學<br>食品科學系<br>100<br>The aim of this study is to separate oligosaccharides (OS) with different degree of polymerization (DP) from hydrolysate of Sargassum sp., Gracilaria sp., and Ulva lactuca polysaccharides (PS), and using chlorsulfonic acid- N, N-dimethylformamide (DMF) method to increase sulfate contents of these OS. The effects of their anticoagulant, anti-platelet aggregation, antiviral activities, and its adsorption performance with intestinal cell line Caco-2 are examined. Sargassum sp., Gracilaria sp., and Ulva lactuca was extracted by 121oC hot water to obtain PS, and th
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Buff, Maximilian [Verfasser]. "Regulation der Aktivität eines Anti-Thrombin-Aptamers und des glmS-Ribozyms mit Licht / von Maximilian C. R. Buff." 2010. http://d-nb.info/1009688685/34.

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Anantha, Krishna T. H. "Anti-thrombotic Secondary Metabolites from Endophytic Fungi of Datura Metel and Cassia Fistula." Thesis, 2017. http://etd.iisc.ac.in/handle/2005/4149.

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Blood coagulation is a process that occurs normally in an animal during bleeding, to prevent the loss of blood from the body and is assisted by two key players -blood platelets and coagulation factors particularly thrombin. When this process becomes extensive, it leads to thrombosis, a condition which can lead to severities such as cardiac failure, brain hemorrhage,renal failure and deep vein thrombosis. Anti-thrombotic drugs which are administered to combat thrombosis can be classified into three categories - anticoagulants, antiplatelet drugs (also known as blood thinners) and fibrinolytic d
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Books on the topic "Anti-thrombin"

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Kessler, Heike. Steuerung und Überwachung der chronischen Hämodialyse mit Thrombin-Antithrombin-III-Komplex (TAT), Fibrinopeptid A (FPA) und Anti-Faktor Xa (Anti-FXa). 1993.

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Stanworth, Simon, and Stuart McKechnie. Pathophysiology of disordered coagulation. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199600830.003.0269.

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Imbalances in the regulation of haemostasis may manifest as bleeding (depletion of pro-coagulant factors) or thrombosis (deficiency of anti-coagulants). Disordered haemostasis is common in critically-ill patients and may result from infection, trauma, haemorrhage, inflammation, organ dysfunction (notably renal and liver dysfunction), or drug therapy. Complex patterns of coagulopathy where both bleeding and prothrombotic tendencies co-exist are well recognized in critical illness. The limitations of standard laboratory coagulation tests to predict bleeding risk, including activated partial thro
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Book chapters on the topic "Anti-thrombin"

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Bavry, Anthony A., and Deepak L. Bhatt. "Anti-thrombin therapy." In Acute Coronary Syndromes in Clinical Practice. Springer London, 2008. http://dx.doi.org/10.1007/978-1-84800-358-3_6.

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Bavry, Anthony A., and Deepak L. Bhatt. "Anti-thrombin therapy." In Managing Acute Coronary Syndromes in Clinical Practice. Springer Healthcare Ltd., 2008. http://dx.doi.org/10.1007/978-1-908517-14-2_6.

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Petralia*, Gloria A., and Ajay K. Kakkar. "Anti-thrombotic Therapy in Cancer Patients." In Thrombin. Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-09637-7_11.

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Lai, K. N., J. Yin, P. Li, and P. Yuen. "Changes of Anti-Thrombin III (AT III), Protein C (PC), and Protein S (PS) in Renal Transplantation." In Current Therapy in Nephrology. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4613-0865-2_131.

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Becker, Richard C., and Frederick A. Spencer. "Thrombin-Directed Therapy." In Fibrinolytic and Antithrombotic Therapy. Oxford University Press, 2006. http://dx.doi.org/10.1093/oso/9780195155648.003.0020.

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Anticoagulant therapy in general is designed to prevent either the generation or activity of thrombin; however, a cell-based model of coagulation provides a physiologic view of individual phases of the process, allowing more specific targets for attenuating the initiation, priming, or propagation of thrombus formation. Future categorization schemes will consider individual coagulation factors, individual sites on a given coagulation factor, and specific phases of coagulation to better identify an agent’s biochemical and physiologic activity. Unfractionated heparin (UFH) is a heterogeneous, neg
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Roshal, Mikhail. "Monitoring of Heparins, Fondaparinux, Direct Thrombin Inhibitors and Oral Anti-Xa Medications." In Transfusion Medicine and Hemostasis. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-397164-7.00151-8.

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Avecilla, Scott T., Mikhail Roshal, Morayma Reyes Gil, and Patrick A. Erdman. "Laboratory Monitoring for Heparins, Fondaparinux, Direct Thrombin Inhibitors, and Oral Anti-Xa Medications." In Transfusion Medicine and Hemostasis. Elsevier, 2019. http://dx.doi.org/10.1016/b978-0-12-813726-0.00159-8.

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Avecilla, Scott T., and Morayma Reyes Gil. "Laboratory Monitoring for Heparins, Fondaparinux, Direct Thrombin Inhibitors, and Oral Anti-Xa Medications." In Transfusion Medicine and Hemostasis. Elsevier, 2025. http://dx.doi.org/10.1016/b978-0-323-96014-4.00093-8.

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N. Magnani, Harry. "Danaparoid Sodium: A Review of Its Use in Hepatic Thrombotic Disorders." In Anticoagulation - Current Perspectives [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.103851.

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Danaparoid sodium is an antithrombotic isolated from porcine mucosa. Its main constituent is a mixture of heparan sulphates that inhibits thrombin generation and also possesses anti-inflammatory and immune-modulatory activity. It has shown safety and efficacy in its main indications of deep venous thrombosis prophylaxis, heparin-induced thrombocytopenia treatment and disseminated intravascular thrombosis treatment. In addition, there are reports of its off-label use for the treatment of portal vein thrombosis in adults and for prevention of the hepatic thrombotic microangiopathies haematogenou
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Conference papers on the topic "Anti-thrombin"

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Visser, A., and D. G. Meuleman. "IRREVERSIBLE INHIBITION OF THE THROMBIN-MEDIATED SIGNAL TRANSFER." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644808.

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The inhibition of the thrombin-mediated signal transfer by a common irreversible inhibitor Z of the factor Xa complex (Xc a) and thrombin has been analysed for the two-step process of the Xc a-triggered formation of thrombin andthe consecutive splitting ok a thrombin-specific substrate S. Assuming that both proteolytic processes follow simple Michaelis—Menten kinetics, that the inhibition reactions are second-order and that the prothrombin and irreversible inhibitor are in excess it can be shown that:1. clotting time (tc) is inversely proportional to the time-averaged thrombin concentration2.
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Björk, I., S. T. Olson, and J. D. Shore. "BINDING OF HEPARIN TO H-KININOGEN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642853.

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The binding of heparin to kininogen was analyzed by competition of kininogen with anti thrombin for high-affinity heparin. Residual heparin binding to anti thrombin was quantified by the accelerating effect on the anti thrombin-thrombin reaction. The rate of the latter reaction was monitored by displacement of the fluorescent probe, p-aminobenzamidine, from the enzyme. A linear dependence of the observed pseudo-first-order rate constant (kobs) for the heparin-accelerated anti thrombin-thrombin reaction on heparin concentration was achieved by use of catalytic amounts (≤30 nM) of heparin, a 20-
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van Dinther, T. G., F. Hol, and D. G. Meuleman. "EFFECT OF VARIOUS HEPARIN(OID)S ON HEPARIN COFACTOR II MEDIATED ANTI-THROMBIN ACTIVITY AND INHIBITION OF THROMBIN GENERATION IN VITRO." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644353.

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The effects of various heparin(oid)s, standard heparin VII (SH), dermatan sulphate (DS), a low molecular weight fraction of heparin (UMW-H), FragminR (FRA), Org 10172 = low molecular weight heparinoid, the fraction of Org 10172 with high affinity for AT-III (HA-10172) and the low affinity fraction (LA-10172) respectively were examined on in vitro thrombin generation and inactivation.Thrombin inactivation in the presence of either heparin cofactor II (HC-II) or anti-thrombin III (AT-III) was assessed with two newly developed assays using the purified cofactors, thrombin and chromogenic substrat
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Rathjen, Deborah A., and Carolyn L. Geczy. "PRODUCTION AND CHARACTERISATION OF A MONOCLONAL ANTIBODY AGAINST HUMAN ANTI-THROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644358.

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To study the role of anticoagulants, particularly antithrombin III (AT III) and heparin, on the activation of coagulation by monocytes/macrophages which have been stimulated with a soluble lymphocyte activation product, macrophage procoagulant inducing factor, we have prepared monoclonal antibodies (MAbs) to human AT III.In fusion experiments, in contrast to wells containing peritoneal feeder cells, positive hybrids were only found in wells containing medium conditioned by the macrophage cell line J774 (Rathjen and Geczy, 1986). Of 5 hybrids which initially produced antibody, only one hybrid,
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Vinazzer, H., and U. Pangraz. "HEPARIN COFACTOR II: A SIMPLE ASSAY METHOD." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644349.

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A photometric assay method for heparin cofactor II (HC II) is described. In a first step antithrombin III (AT III) in plasma is blocked by an anti human AT III immunoglobuline from goats. After dilution of this plasma with Tris buffer pH 8.4 containing 3 IU/ml heparin and addition of thrombin the remaining thrombin activity is measured by use of the chromogenic substrate S-2238 Kabi. The following preliminary experiments were carried out: Variation of the amount of anti-AT III added to plasma resulted in complete inactivation of 1.25 units AT III by 1.0 ml of the inhibitor. Incubation of 1 ml
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Galustian, Christine, Teresa Melchionna, Osamu Ukimura, Inderbir Gill, Richard Smith, and Prokar Dasgupta. "Abstract 673: Use of membrane-tethered anti-thrombin compounds in prostate cancer therapy." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-673.

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Lee, Jisook, Alexandra Borboa, Andrew Baird, and Brian Eliceiri. "Abstract A21: Thrombin-processed Ecrg4 recruits myeloid cells and induces anti-tumorigenic inflammation." In Abstracts: AACR Special Conference on Cellular Heterogeneity in the Tumor Microenvironment; February 26 — March 1, 2014; San Diego, CA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.chtme14-a21.

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Kenneally, D. A., P. J. Thurlow, and J. M. Cornellan. "MONOCLONAL ANTIBODY (ANTI-2B6D4) TO PLASMA FIBRONECTIN INHIBITS COLLAGEN AND THROMBIN INDUCED AGGREGATION OF WASHED PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643861.

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Fibronectins(Fns) constitute a family of large glycoproteins which are known to bind to a wide range of biological molecules eg.collagen, gelatin, fibrin, heparin and DNA,and to many cells including platelets via discrete structural domains. A murine monoclonal antibody (anti-2B6D4) produced by imnunizing BALB/c mice with plasma fn, was used to study the structure and function of fn and its platelet interaction Anti-2B6D4 reacted specifically with plasma fn was unreactive with FVIII/vWF,BTG,PF4 collagen and fibrinogen nor was it reactive with platelets (unstiraulated), human PBLs or a range of
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Samama, J. P., M. Delarue, D. Moras, M. Petitou, J. C. Lormeau, and J. Choay. "CRYSTALLOGRAPHIC INVESTIGATION OF ANTITHROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643765.

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The plasma protein inhibitor anti thrombin III in its native form has been crystallized using standard techniques.The crystals diffract to about and belong to space group P41212 with cell parameters:a = b = 90.6&lt;, c = 380.7&lt;.The asymmetric unit contains three molecules of anti thrombin III.The self rotation function computed with the native data set indicates the presence of a non crystallographic three fold axis. Cross rotation function calculations using themodel of the cleaved α1,-antitrypsin (H. Loebermann at.,J. Mol. Biol.(1985) 177, 531) suggests tertiary structuresimilarities betw
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Schoen, P., H. C. Hemker, and T. Lindhoubt. "INHIBITION OF FACTOR Xa AND THROMBIN BY ANTITHROMBIN III AND HEPARIN DURING HUMAN PROTHROMBIN ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643766.

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Abstract:
Prothrombin-catalyzed human prothrombin activation results in the generation of thrombin and meizothrombin- des FI (MDF1) as was demonstrated by an immunoblot technique. Theheparin-independent second order rate -.onstants of inhibition of both thrombin and MDF1were 3.7 x 105 M-1min-1, whereas the rate constant of inhibition of purified thrombin was 6.5 x 105 M-1min-1 . In the presence of heparin the decay of amidolytic thrombin activity appeared to be bi-exponential and could be modelled by a 4-parameter equation. Fitting the experimental data to this equation gave the pseudo-first-order rate
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