Relevant bibliographies by topics / Antithrombin III

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  2. Dissertations / Theses
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Academic literature on the topic 'Antithrombin III'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 August 2024

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Journal articles on the topic "Antithrombin III"

1

Sakuragawa, Nobuo, Shin-ichi Kondo, Masahiko Katoh, Kaoru Takahashi, and Takehiko Koide. "Antithrombin III microheterogeneity in antithrombin III deficiency and in the antithrombin III abnormality, “antithrombin III toyama”." Thrombosis Research 47, no. 2 (July 1987): 147–53. http://dx.doi.org/10.1016/0049-3848(87)90371-9.

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Beresford, Charles H., and Maurice C. Owen. "Antithrombin III." International Journal of Biochemistry 22, no. 2 (January 1990): 121–28. http://dx.doi.org/10.1016/0020-711x(90)90172-y.

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George, PM, P. Pemberton, IC Bathurst, RW Carrell, HL Gibson, S. Rosenberg, RA Hallewell, and PJ Barr. "Characterization of antithrombins produced by active site mutagenesis of human alpha 1-antitrypsin expressed in yeast." Blood 73, no. 2 (February 1, 1989): 490–96. http://dx.doi.org/10.1182/blood.v73.2.490.490.

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Abstract Both congenital and acquired antithrombin-III (AT-III) deficiencies are amenable to replacement therapy. We describe two antithrombins produced by recombinant DNA techniques from human alpha 1-antitrypsin (alpha 1AT) cDNA in yeast. Alteration of the alpha 1AT active site, replacing methionine 358 with arginine, results in a thrombin inhibition rate similar to that of heparin-activated AT-III. Alteration of two further residues, to give a five-residue sequence identical to AT-III, does not increase this rate further. Neither antithrombin is activated by heparin; both are unglycosylated and have shorter in vivo half-lives (t1/2) than human alpha 1AT. These antithrombins should be suitable for therapeutic replacement of AT-III in cases of congenital deficiency and in conditions associated with acquired AT-III deficiency, such as disseminated intravascular coagulation.
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George, PM, P. Pemberton, IC Bathurst, RW Carrell, HL Gibson, S. Rosenberg, RA Hallewell, and PJ Barr. "Characterization of antithrombins produced by active site mutagenesis of human alpha 1-antitrypsin expressed in yeast." Blood 73, no. 2 (February 1, 1989): 490–96. http://dx.doi.org/10.1182/blood.v73.2.490.bloodjournal732490.

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Both congenital and acquired antithrombin-III (AT-III) deficiencies are amenable to replacement therapy. We describe two antithrombins produced by recombinant DNA techniques from human alpha 1-antitrypsin (alpha 1AT) cDNA in yeast. Alteration of the alpha 1AT active site, replacing methionine 358 with arginine, results in a thrombin inhibition rate similar to that of heparin-activated AT-III. Alteration of two further residues, to give a five-residue sequence identical to AT-III, does not increase this rate further. Neither antithrombin is activated by heparin; both are unglycosylated and have shorter in vivo half-lives (t1/2) than human alpha 1AT. These antithrombins should be suitable for therapeutic replacement of AT-III in cases of congenital deficiency and in conditions associated with acquired AT-III deficiency, such as disseminated intravascular coagulation.
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5

Owen, MC, JY Borg, C. Soria, J. Soria, J. Caen, and RW Carrell. "Heparin binding defect in a new antithrombin III variant: Rouen, 47 Arg to His." Blood 69, no. 5 (May 1, 1987): 1275–79. http://dx.doi.org/10.1182/blood.v69.5.1275.1275.

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Abstract Antithrombin III (AT-III) Rouen is a hereditary abnormal antithrombin with normal progressive inhibitory activity and reduced heparin cofactor activity. It was isolated from the plasma of a woman who suffered a sudden idiopathic sensorineural hearing loss and balance impairment. There was no familial history of thrombosis. By heparin- Sepharose chromatography, AT-III Rouen was separated from the normal antithrombin on elution with increasing concentrations of NaCl. AT-III Rouen eluted earlier than is normal at both pH 7.4 and pH 6.0. At the lower pH, the antithrombins bound more avidly to the column, with the abnormal AT-III eluting closer to the normal than at the higher pH. Two- dimensional peptide mapping of tryptic and Staphylococcus aureus V8 protease digests of carboxymethylated antithrombins was performed on thin-layer silica plates. The abnormal peptide was located by tryptophan staining, and amino acid analysis and sequence studies demonstrated a substitution of an arginine at residue 47 for a histidine. Results from this study suggest that replacement of arginine 47 by a partially positively charged histidine has less effect on the heparin binding affinity than dose replacing it with a neutral cysteine side chain as in AT-III Toyama, in which no heparin binding was observed. In addition, heparin binding per se is not a sufficient condition to activate AT-III.
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Owen, MC, JY Borg, C. Soria, J. Soria, J. Caen, and RW Carrell. "Heparin binding defect in a new antithrombin III variant: Rouen, 47 Arg to His." Blood 69, no. 5 (May 1, 1987): 1275–79. http://dx.doi.org/10.1182/blood.v69.5.1275.bloodjournal6951275.

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Antithrombin III (AT-III) Rouen is a hereditary abnormal antithrombin with normal progressive inhibitory activity and reduced heparin cofactor activity. It was isolated from the plasma of a woman who suffered a sudden idiopathic sensorineural hearing loss and balance impairment. There was no familial history of thrombosis. By heparin- Sepharose chromatography, AT-III Rouen was separated from the normal antithrombin on elution with increasing concentrations of NaCl. AT-III Rouen eluted earlier than is normal at both pH 7.4 and pH 6.0. At the lower pH, the antithrombins bound more avidly to the column, with the abnormal AT-III eluting closer to the normal than at the higher pH. Two- dimensional peptide mapping of tryptic and Staphylococcus aureus V8 protease digests of carboxymethylated antithrombins was performed on thin-layer silica plates. The abnormal peptide was located by tryptophan staining, and amino acid analysis and sequence studies demonstrated a substitution of an arginine at residue 47 for a histidine. Results from this study suggest that replacement of arginine 47 by a partially positively charged histidine has less effect on the heparin binding affinity than dose replacing it with a neutral cysteine side chain as in AT-III Toyama, in which no heparin binding was observed. In addition, heparin binding per se is not a sufficient condition to activate AT-III.
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7

Preiss, Dieter Ulrich, Delawer Abdullah, Bruno Eberspächer, and Karlheinz Wilhelm. "Safety of virus inactivated antithrombin III concentrate ANTITHROMBIN III IMMUNO (AT III)." Thrombosis Research 65, no. 6 (March 1992): 677–86. http://dx.doi.org/10.1016/0049-3848(92)90107-l.

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Menache, Doris. "Antithrombin III Concentrates." Hematology/Oncology Clinics of North America 6, no. 5 (October 1992): 1115–20. http://dx.doi.org/10.1016/s0889-8588(18)30298-3.

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9

Beresford, C. H. "Antithrombin III deficiency." Blood Reviews 2, no. 4 (December 1988): 239–50. http://dx.doi.org/10.1016/0268-960x(88)90013-6.

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Tomar, AS, M. Daga, N. Kaushik, and PremKumar Singh. "Antithrombin III Deficiency." Annals of Cardiac Anaesthesia 6, no. 1 (2003): 80. http://dx.doi.org/10.4103/0971-9784.38737.

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Dissertations / Theses on the topic "Antithrombin III"

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Oldeen, Molly Elisabeth. "Optimizing Anticoagulation Therapy in ECMO Patients using Antithrombin III." Thesis, The University of Arizona, 2012. http://hdl.handle.net/10150/228500.

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One of the most fundamental aspects of extracorporeal membrane oxygenation (ECMO) is maintaining proper anticoagulation management in order to prevent hemorrhagic or thrombotic events. Anticoagulation on ECMO is most commonly achieved with the use of unfractionated heparin to maintain a minimum anticoagulation level as monitored by activated clotting time (ACT). Heparin's main effect is exerted by binding to and potentiating antithrombin III. Many factors may contribute to a sub-therapeutic ATIII level that may decrease the effectiveness of heparin. A retrospective record review was performed on all adult ECMO patients at the University of Arizona Medical Center between 2008 and 2011, in order to determine optimal ATIII levels for maintaining proper anticoagulation. In addition, we investigated correlations between ATIII levels and hemorrhagic and/or thrombotic events. Variables measured include, ACTs, heparin dose, ATIII dose, ATIII levels, blood product use, and adverse events. Thirty-five patients received ATIII over the course of the ECMO run. Six patients did not receive ATIII and they were found to have used significantly more blood products than those who did receive ATIII. Also, heparin dose dropped significantly 24h after the first dose of ATIII. There is a significant positive correlation between the amount of ATIII given per day and the amount of packed red blood cells transfused per day. The results suggest an ideal therapeutic range of ATIII dosing, where lack of or too much ATIII administration can lead to excessive bleeding.
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Zilker, Susanne. "Aktivitätsgesteuerte Therapie der schweren chirurgischen Sepsis mit Antithrombin III." Diss., lmu, 2009. http://nbn-resolving.de/urn:nbn:de:bvb:19-99495.

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Kittel, Florina Luisa [Verfasser], and Hinnak [Akademischer Betreuer] Northoff. "Schwingquarzbasierte Bestimmung von Antithrombin III / Florina Luisa Kittel ; Betreuer: Hinnak Northoff." Tübingen : Universitätsbibliothek Tübingen, 2015. http://d-nb.info/1197057986/34.

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Kittel, Florina [Verfasser], and Hinnak [Akademischer Betreuer] Northoff. "Schwingquarzbasierte Bestimmung von Antithrombin III / Florina Luisa Kittel ; Betreuer: Hinnak Northoff." Tübingen : Universitätsbibliothek Tübingen, 2015. http://d-nb.info/1197057986/34.

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Hagel, Stefan. "Protein C- und Antithrombin III-Aktivität : Stellenwert bei der Diagnose und Verlaufsbeurteilung unterschiedlicher systemischer Entzündungssyndrome bei kritisch kranken Patienten /." Saarbrücken VDM Verlag Dr. Müller, 2006. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=015040669&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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Pfannenschmidt, Gerd. "Der Effekt von Antithrombin III auf die pulmonalvaskuläre Freisetzung von Big Endothelin-1, Endothelin-1 und Prostanoiden unter septischen und nichtseptischen Bedingungen sowie seine Mechanismen." Doctoral thesis, Humboldt-Universität zu Berlin, Medizinische Fakultät - Universitätsklinikum Charité, 2000. http://dx.doi.org/10.18452/14540.

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Die Arbeit sollte klären, ob die pulmonalprotektiven Effekte von AT III bei LPS-induziertem ARDS auch auf einer Stimulation der pulmonalvaskulären PGI2-Freisetzung beruhen. Die Freisetzung von Big ET-1 und ET-1 unter septischen Bedingungen sollte quantifiziert sowie mögliche Effekte von AT III auf diese Freisetzung untersucht werden. Dabei wurde das Modell der isolierten Rattenlunge verwendet. Die Perfusion der Lunge mit LPS führte zu einer Steigerung der Kon-zentration von 6-Keto-PGF1(, dem stabilen Metaboliten von PGI2, auf das 1,6fache und der Konzentration von TxB2, dem stabilen Metaboliten von TxA2, auf das 2,9fache gegenüber der Kontrollgruppe. Die Konzentration von ET-1 erhöhte sich unter LPS auf das 1,6fache, während der Big ET-1 Spiegel konstant blieb. Die Gabe von AT III hatte keinen Effekt auf die Freisetzung von PGI2 und TxA2. Die kombinierte Gabe von LPS und AT III wirkte ebenso wie die Gabe von LPS allein. Die Konzentrationen von Big ET-1 und ET-1 erhöhten sich unter 2 U/ml AT III auf das 1,7- bzw. 1,2fache und unter 5 U/ml AT III auf das 1,6- bzw. 1,3fache gegen-über den Kontrollen. Die kombinierte Gabe von LPS und AT III führte zu einem signifikant höheren Big ET-1-Spiegel vom 2,6fachen des Basalwertes, während sich die Konzentration von ET-1 nicht von der unter LPS bzw. AT III allein unterschied. Die Gabe von Cicaprost, einem stabilen synthetischen PGI2-Analogon, beeinflußte weder die basale noch die durch 2 U/ml AT III und 50 µg/ml LPS stimulierte Big-ET-1- und ET-1-Freisetzung. Nicardipin, ein Blocker der L-Typ-Kalzium-Kanäle, Heparin und N-Acetyl-Heparin, ein nicht an AT III bindendes Heparin, antagonisierten jeweils den stimulierenden Effekt von AT III auf die Big-ET-1- und ET-1-Freisetzung komplett. Staurosporin, ein Proteinkinase C-Inhibitor und Genistein, ein Tyrosinkinase-Inhibitor hatten keinen Effekt auf die durch AT III stimulierte Big-ET-1- und ET-1-Freisetzung. SCHLUßFOLGERUNGEN: Das für den protektiven Effekt des AT III bei ARDS verantwortlich gemachte PGI2 scheint nichtpulmonalen Ursprungs zu sein. Eine PGI2-mediierte Hemmung der pulmonalen ET-1-Sekretion war nicht zu beobachten und scheint somit nicht am protektiven Effekt des AT III beim septischen ARDS beteiligt zu sein. Der beobachtete stimulierende Effekt des AT III auf die Freisetzung der pulmonalen Endotheline ist von möglicher pathophysiologischer Relevanz, da er die erwähnte protektive Wirkung des AT III mit hoher Wahrscheinlichkeit abschwächt. Dieser stimulierende Effekt des AT III scheint dabei an der intakten Rattenlunge weder von der Proteinkinase C noch von Tyrosinkinasen vermittelt zu sein. Weiterhin ist festzustellen, daß die stimulierende Wirkung des AT III auf die pulmonalvaskuläre Freisetzung von Big ET-1 und ET-1 von einem Kalziumeinstrom durch L-Typ-Kalzium-Kanäle und damit von der intrazellulären Kalziumkonzentration abhängig ist. Wie die gleiche Wirksamkeit von Heparin und N-Azetyl-Heparin zeigt, erfordert die Blockade des AT-III-Effektes durch die Heparine keine direkte Bindung an AT III, was auf die zusätzliche Rolle der intrazellulären Kalziumfreisetzung über IP3 hinweist.
The aim of the present study was to clarify if the pulmonary protective effects of AT III in LPS-induced ARDS can be attributed to a stimulation of the pulmonary vascular release of PGI2. The pulmonary vascular release of big ET-1 and ET-1 under septic conditions and the possible influence of AT III was to be investigated. To this end, we used the model of the isolated perfused rat lung. Exposure of the lung to LPS increased the release of 6-Keto-PGF1(, the stable metabolite of PGI2, 1.6fold and the production of TxB2, the stable metabolite of TxA2, 2.9fold compared with control lungs. The release of ET-1 increased 1.6fold under LPS, whereas the concentration of big ET-1 was unchanged. The application of AT III had no effect on the release of PGI2 and TxA2. The effects following combined application of LPS and AT III were similar to the effects of LPS alone. Compared with controls, AT III, at 2 U/ml, increased the perfusate levels of big ET-1 and ET-1 1.7fold and 1.2fold, respectively; the administration of 5 U/ml AT III raised big ET-1 and ET-1 1.6fold and 1.3fold, respectively. Combined application of LPS and AT III resulted in a 2.6fold rise of big ET-1 levels compared with controls, whereas concentrations of ET-1 did not differ from those in the presence of LPS or AT III alone. Cicaprost, a stable PGI2 analogue, affected neither the basal nor the AT III plus LPS-stimulated release of big ET-1 and ET-1. Nicardipin, an L-type calcium channel blocker, heparin and N-acetyl heparin, a heparin derivative devoid of AT III affinity, each antagonized completely the AT III-stimulated increase in big ET-1 and ET-1 levels. Staurosporin, an inhibitor of protein kinase C, and genistein, an inhibitor of tyrosine kinases, did not influence the AT III effects on endothelins. CONCLUSIONS: In ARDS, the well-known rise in plasma PGI2 in response to AT III obviously originates from non-pulmonary sources. PGI2 does not suppress the pulmonary ET-1 secretion; therefore, this mechanism seems not involved in the AT III-induced lung protection during septic ARDS. The AT III-mediated stimulation of the release of pulmonary endothelins is of potential pathophysiological relevance, because it may blunt the protective effects of AT III in ARDS. In the intact rat lung, this stimulatory effect of AT III is mediated neither by protein kinase C nor by tyrosine kinases. Moreover, the observed effect of AT III on pulmonary endothelins is based on calcium influx through L-type calcium channels and depends on the intracellular calcium activity. The equipotency of heparin and N-acetyl heparin in inhibiting the AT III action demonstrates that direct binding of AT III is not essential for the blocking effect of heparins. This fact points to additional involvement of an IP3-dependent intracellular calcium release.
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Yamashiro, Kenji. "Inhibitory Effects of Antithrombin III against Leukocyte Rolling and Infiltration during Endotoxin-induced Uveitis in Rats." Kyoto University, 2003. http://hdl.handle.net/2433/148459.

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Fazavana, Judicaël. "Développement d’une antithrombine modifiée inactive comme antidote des anticoagulants hépariniques." Thesis, Paris 11, 2012. http://www.theses.fr/2012PA114855/document.

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Les héparines regroupant les héparines standards (HNF), les héparines de bas poids moléculaire(HBPM), et le fondaparinux, sont des médicaments anticoagulants. Ils potentialisent l’antithrombine (AT) : un inhibiteur physiologique de la coagulation. Leur utilisation en thérapeutique est associée à un risque hémorragique majeur. Actuellement, le sulfate de protamine est le seul antidote disponible vis-à-vis des HNF. Il est partiellement efficace vis-à-vis des HBPM, et n’a aucun effet contre le fondaparinux, qui n’a pas d’antidote jusqu’à présent. C’est dans ce contexte que nous proposons des AT modifiées inactives, mais capables de se lier aux molécules d’héparines. Ces AT déplaceraient les molécules d’héparines de l’AT plasmatique, et neutraliseraient leur effet anticoagulant. Pour produire de telles AT, nous avons choisi une approche recombinante et une approche chimique. Dans la première approche, nous avons exprimé le variant AT-N135Q-Pro394. Ce variant possède une activité anti-Xa ou anti-IIa inférieure à 0,02% en présence de dérivés hépariniques, et une affinité à l’héparine 3 fois meilleure, comparée à l’AT plasmatique. En revanche, dans l’approche chimique, nous avons modifié l’AT plasmatique par la 2,3-butanedione (AT-BD), un réactif chimique de caractérisation des arginines. Contrairement au variant, cette AT-BD a une perte d’activité anticoagulante modérée, puis une affinité à l’héparine 20 fois meilleure, comparée à l’AT plasmatique. Malgré ces différences de propriétés biochimiques, ces 2 AT modifiées neutralisent d’une façon similaire les héparines in vitro et sur un modèle murin. Par ailleurs, à l’inverse du sulfate de protamine, nos antidotes n’ont pas d’activité anticoagulante propre sur un test de céphaline activée. Ainsi, ce travail de thèse a permis non seulement de proposer les premiers et les seuls antidotes spécifiques au fondaparinux décrits, mais aussi des antidotes alternatifs pour tous les anticoagulants hépariniques
Unfractionnated heparin (UFH), low molecular weight heparins (LMWH), and fondaparinux are used therapeutically as anticoagulants. They potentiate antithrombin (AT): a physiological inhibitor of coagulation. Their therapeutic use is associated with a major risk of bleeding. Currently, protamine sulfate is the only antidote available for UFH. It is partially effective for LMWH, and has no effect against fondaparinux, which has no antidote. So, we propose modified inactive AT, but able to bind heparin molecules as antidote of these heparins. These molecules would compete with plasmatic AT for binding to heparins, and neutralize their anticoagulant effect. To produce that AT, we realized a genetic approach and a chemical approach. In the first approach, we expressed the variant AT-N135Q-Pro394 that had an anti-Xa or anti-IIa activity below 0.02% in the presence of heparins, and heparin affinity three times higher, compared to the plasmatic AT. In the chemical approach, we modified the plasmatic AT by 2,3-butanedione (AT-BD), a chemical reagent for arginin’s characterization. The AT-BD had a moderate loss of anticoagulant activity, and a heparin affinity 20 times higher, compared to the plasmatic AT. Despite these differences in biochemical properties, these two modified AT neutralize similarly heparins in vitro and in a mouse model. Moreover, unlike protamine sulfate, our antidotes had not an intrinsic anticoagulant effect in activated partial thromboplastin test. Thus, this PhD-work offers the first and the only specific antidote described to fondaparinux, and it can be used too alternatively for all anticoagulant heparins
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Hashim, R. Bt. "The use of fluorescent probes in the study of the interaction of the interaction of heparin with antithrombin III and polycations." Thesis, University of Salford, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.356175.

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Pfannenschmidt, Gerd. "Der Effekt von Antithrombin-III auf die pulmonalvaskuläre Freisetzung von Big-Endothelin-1, Endothelin-1 und Prostanoiden unter septischen und nichtseptischen Bedingungen sowie seine Mechanismen." [S.l.] : [s.n.], 2000. http://deposit.ddb.de/cgi-bin/dokserv?idn=960868755.

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Books on the topic "Antithrombin III"

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Sas, Géza. The biology of antithrombins. Boca Raton, Fla: CRC Press, 1990.

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Jepsen, Kerstin. Antithrombin-III-Plasmaspiegel [Antithrombin-Plasmaspiegel] bei verschiedenen intermedizinischen Erkrankungen. [s.l.]: [s.n.], 1988.

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Sas, Géza. The biology of antithrombins. Boca Raton, Fla: CRC Press, 1990.

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Oehm, Horst. Antithrombin III: Seine bedeutung für die Therapie der Verbrauchskoagulopathie und die Wertigkeit der Antithrombin-III-Spiegelbestimmungen [Antithrombin-Spiegelbestimmungen] in der Diagnostik thrombophiler Zustände. [s.l.]: [s.n.], 1987.

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Ramm, Inga. Die Wirkung des Heparin-Antithrombin-III-Komplexes auf die Fibroblastenproliferation. [s.l.]: [s.n.], 1997.

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Pfundstein, Christof Johannes. Hochdosierte Antithrombin III-Behandlung polytraumatisierter Patienten: Ergebnisse einer prospektiven, randomisierten, Placebo-kontrollierten Doppelblindstudie. [s.l.]: [s.n.], 1999.

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Janssen, Gudrun. Verhalten und prognostische Bedeutung von Fibrinogen, Faktor XIII, Antithrombin III und Thrombozyten bei Verbrannten. [s.l.]: [s.n.], 1985.

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Ramirez, Pablo Antonio Rivera. Messung der Antithrombin III-aktivität bei der Katze: Referenzbereich und Veränderung bei verschiedenen Erkrankungen. Hannover: s.n., 1997.

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Sharma, Anupama. A comparison of the binding abilities of human kidney heparan sulphate and heparin glycosaminoglycans for antithrombin III. Manchester: University of Manchester, 1995.

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Quendt, Joachim. Der perioperative Verlauf von Faktor I, VIII, X und XII sowie Antithrombin III und [alpha]2-Makroglobulin [Alpha-Makroglobulin] bei Hüftgelenkstotalendoprothesenimplantation. [s.l.]: [s.n.], 1987.

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Book chapters on the topic "Antithrombin III"

1

Schuster, H. P., and S. Knaub. "Antithrombin III." In Intensivtherapie bei Sepsis und Multiorganversagen, 191–208. Berlin, Heidelberg: Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-662-07962-1_8.

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Scharnagl, Hubert, Winfried März, Markus Böhm, Thomas A. Luger, Federico Fracassi, Alessia Diana, Thomas Frieling, et al. "Antithrombin III/AT3." In Encyclopedia of Molecular Mechanisms of Disease, 109. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_6347.

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Harenberg, J. "Thrombin—antithrombin III complexes." In ECAT Assay Procedures A Manual of Laboratory Techniques, 117–23. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2992-3_14.

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Müller, G. "Erworbene Antithrombin-III-Mangelzustände." In 21. Hämophilie-Symposion, 247–51. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76764-7_52.

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Schricker, K. Th, B. Neidhardt, and E. Schricker. "Zur Frage der Antithrombin III-Substitution bei erworbenem Antithrombin III-Mangel." In Neue Entwicklungen in der Transfusionsmedizin, 62–66. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-77443-0_7.

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Inthorn, D. "Therapie mit Proteinaseinhibitoren. Antithrombin III." In Intensivtherapie bei Sepsis und Multiorganversagen, 124–40. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-07958-4_7.

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Inthorn, D. "Therapie mit Proteinaseinhibitoren. Antithrombin III." In Intensivtherapie bei Sepsis und Multiorganversagen, 91–107. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-07960-7_6.

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Conard, J. "Antithrombin III activity and antigen." In ECAT Assay Procedures A Manual of Laboratory Techniques, 77–84. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2992-3_10.

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9

Laschke, Matthias W., J. N. Hoffmann, B. Vollmar, D. Inthorn, F. W. Schildberg, and M. D. Menger. "Heparin-Antithrombin-III-Antagonismus bei Endotoxinämie." In Chirurgisches Forum 2002, 357–59. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-56158-0_91.

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Bock, Susan Clark. "Antithrombin III Genetics, Structure and Function." In Recombinant Technology in Hemostasis and Thrombosis, 25–45. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3698-7_3.

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Conference papers on the topic "Antithrombin III"

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Knoller, S., and N. Savion. "MODULATION OF ANTITHROMBIN III ACTIVITY AND ANTITHROMBIN III-THROMBIN COMPLEXES BINDING TO CULTURED CELLS BY MONOCLONAL ANTIBODIES AGAINST ANTITHROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644361.

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Two monoclonal antibodies (mAb's) against antithrombin III (ATIII) were characterized with respect to their ability to interfere with ATIII activity. AT III activity was measured by its ability to inhibit the amidolitic activity of thrombin on the substrate BCP-100. Incubation of 150 ng of ATIII with 28pg mAb A36R2 prior to addition of 50 ng thrombin totally abolishes the inhibitory effect of ATIII on thrombin. Incubation of 200ng of ATIII with 10 μg of mAb B26R4 prior to addition of 75 ng thrombin raises the inhibitory effects of ATIII from 37% to 100%. We examined the effect of these mAb's on binding of antithrombin III-thrombin (ATIII-Th) complexes to bovine corneal endothelial cells. 120 pg/ml mAb's are reacted with 2 μg/ml ATIII-Th complexes prior to their addition to the cells. mAb A36R2 completely blocks ATIII-Th complexes binding. In contrast, mAb B26R4 enhances binding up to 250% of the control binding.We conclude that mAb A36R2 prevents binding of thrombin to ATIII by recognizing an epitope on ATIII close to thrombin binding site or that its binding to ATIII induces a conformational change in the thrombin binding site thus it no longer recognizes thrombin. mAb B26R4 has a heparin-like effect on ATIII: Its binding to ATIII induces conformational changes which improve thrombin binding to ATIII. There is a correlation between inhibition and enhancement of thrombin binding to ATIII and of ATIII-Th complexes binding to cells by the two mAb's. These mAb's may provide a new tool to control the activity of ATIII and to identify the cellular binding site on the ATIII-Th complex.This research was supported by a grant from the National Council for Research and Development, Israel and G.S.F. München, Germany.
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de Moerloose, Ph, G. Reber, Ph Minazio, and C. A. Bouvier. "ANTITHROMBIN III GENEVA : AN HEREDITARY ABNORMAL ANTITHROMBIN III (AT III) WITH DEFECTIVE HEPARIN COFACTOR ACTIVITY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644367.

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A 43-year old man presented a pulmonary embolism. Despite a negative family history for thromboembolic disorders, the unusual circumstances of apparition and the relatively young age of the patient prompted us to study carefully the coagulation parameters. Routine coagulation tests, as well as plasminogen, alpha-2-anti-plasmin, protein C and protein S were all within normal range. Biological and immunological assays of AT III were performed on 12 members of the family and showed a low AT III activity in the propositus and other members of this family (mean 50%), but normal immunologic levels. Crossed immunoelectrophoresis in absence of heparin showed a normal pattern, but in presence of heparin showed an abnormal peak as compared with controls. Kinetics experiments showed a normal inhibition of Xa and 11a in absence of heparin, but abnormal in presence of heparin. An affinity chromatography on heparin Sepharose revealed two populations of AT III, one of which was devoid of heparin cofactor activity.The toponym AT III Geneva is proposed for this new familial abnormal AT III with defective heparin cofactor activity. This family confirms the low incidence of thromboembolic events reported in this type of AT III variant.
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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<, c = 380.7<.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 between the two plasma proteins.This is in agreement with the already described primary sequence homology of these glycoproteins but at variance with the model of active α1-anti trypsin inferred from the previous studies on the cleaved molecule.The technical assistance of M. Maman is deeply appreciated.
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Asakura, S., N. Yoshida, and M. Matsuda. "MONOCLONAL ANTIBODIES AGAINST THROHBIN-ANTITHROMBIN III COMPLEX: EPITOPE SPECIFICITY AND EFFECT ON THROMBIN-ANTITHROMBIN III INTERACTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643673.

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Among monoclonal antibodies (MCA´s) raised against human thrombin (T)-antithrombin m (AT) complex (TAT), two MCA´s designated as JITAT-16 and 17 with high affinity, Kd = 4.6nMand 4.1 nfi, respectively, were selected and characterized for specificity and functions. Their respective immunoglobulin subclasses are IgGi and IgG2a, and epitopes were found to be different from each Dther as shown by crisscross inhibition experiments. Immuno-alotting of normal plasma and serum electrophoresed on non-SDS aolyacrylamide gel showed that these antibodies reacted with normal serum but not with plasma. This was verified by an anzyme-linked differential antibody immunosorbent assay using aither one of the MCA´s as the first antibody and the other MCA labeled with peroxidase as the second one. By immunoblotting after SDS-PAGE, we found that both antibodies reacted with TAT, nut not with its respective nascent constituent, AT or T. However, they reacted with reactive site-cleaved AT (or thrombin-nodified AT, ATM) and also a complex of AT with activated factor K (Xa-AT). These results indicate that both of these antibodies recognize enzyme-treated forms of AT, including AT molecules :omplexed with enzymes reversibly or irreversibly as well as ATM. Jpon incubation of T with AT in the presence of JITAT-16, T activity remained nearly unchanged and formation of irreversible rAT did not proceed as expected. Moreover, AT was preferentially :onverted to ATM. When JITAT-16 was added after completion of FAT formation, however, neither recovery of T activity nor generation of ATM was observed. These findings were not obtained vhen JITAT-17 had been substituted for JITAT-16. These data suggest that JITAT-16 may have converted AT from an inhibitor to a substrate for T after having recognized a possible intermediate reversible complex of AT with T. Undoubtedly, in the presence of a polyclonal antibody against AT, neither TAT formation nor ATM neneration was observed at all. The mechanism of the unique Function of JITAT-16 has not been fully clarified as yet, but this antibody seems to give us new information on the kinetic study of TAT formation and ATM generation when AT was allowed to react with enzymes.
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Baruch, D., J. Franssen, H. C. Hemker, and T. Lindhout. "THE ROLE OF HEPARIN CHARGE DENSITY IN THE ANTITHROMBIN III-DEPENDENT AND ANTITHROMBIN III-INDEPENDENT INACTIVATION OF THROMBIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644357.

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The dependence of the anticoagulant properties of heparin upon charge density may reflect structural factors that are important in anti-thrombin effect. We have previously demonstrated that in the absence of antithrombin III (AT III) unfractionated heparin inhibits the catalytic effect of thrombin upon platelet activation. In the present study we evaluated the thrombin-binding properties of heparin fractions obtained by ion-exchange chromatography on DEAE-Sephacei. We found that these fractions were able to bind to thrombin with an affinity that increased with their charge density. This was shown by their inhibitory effect in the absence of AT III on thrombin-catalyzed platelet factor Va formation and by the ability of active site blocked thrombin to prevent the heparin-dependent inactivation of thrombin by AT III. However, their increase in charge density and thus affinity for thrombin was found to go along with an increase in AT III-binding sites, as measured by the heparin-dependent increase of the intrinsic fluorescence of AT III. Moreover all heparin fractions showed the same specific antithrombin activity when the molar concentration of AT III-binding heparin was taken into account. We also investigated the thrombin-binding properties of two heparin fractions obtained by affinity chromatography on AT III-Sepharose. The AT III low affinity fraction was practically devoid of any inhibitory effect on the rate of the thrombin-catalyzed factor Va formation, indicating a low, if any, affinity for thrombin. In contrast the AT III-independent inhibition of thrombin was completely recovered from the AT III high affinity fraction. In addition, we also established that when the heparin fraction from the DEAE-Sephacel column, with the lowest charge density and very low in AT III binding material, was modified by the incorporation of sulfate groups so as to achieve a higher charge density, it obtained a higher affinity for thrombin but this modification caused the loss of half the AT III binding sites. In conclusion, it is apparent that fractionation of crude heparin on a DEAE-Sephacel column or on an AT III-Sepharose column does not result exclusively in a separation of either the thrombin-binding or the AT III-binding heparin fractions.
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Karges, H. E., G. Zettlemeiβl, H. Naumann, U. Eberhard, and M. Bröker. "PURIFICATION AND CHARACTERIZATION OF GENTECHNOLOGICALLY PREPARED ANTITHROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643684.

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Isolation and purification of antithrombin III (AT III) by affinity chromatography on immobilized heparin is a standard method for the large scale preparation of this protein from human or animal plasma. Hence, after AT III became available by gentechnological methods, we tried to adapt this procedure for the isolation of AT III from supernatants of mammalian- and yeast-cells. Indeed, it was possible to use this method also for the isolation of the recombinant gene products. Since, however, the cell growth media contain heterologous protein or peptide mixtures like fetal calf serum, the method had to be improved to avoid the adsorption of non human proteins or peptides. We are now able to purify AT III from CHO-cell-superna-tants to more than 95 % purity. The characterization of this AT III-product by double immuno diffusion revealed that it is immunologically totally identical with the authentic material from plasma. AT III antigen content, progressive inhibitor activity and heparin cofactor activity compare very well in the final product; hence, it is totally active compared to AT III from plasma.In polyacrylamidegel electrophoresis most of the material migrated differently to the authentic material showing 9 bands in equal distance to each other, instead four in the At III from plasma. After degradation with sialinidase from both AT III preparations identical cleavage products were obtained migrating predominantly as a single band. Hence, the electrophoretic heterogeneity seems to be due to a different degree of sialinyla-tion of the products.
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soons, H., T. Jansen-claessen, G. C. Tans, and H. C. Hemker. "HEPARIN CATALYZED FACTOR XIa INHIBITION BY ANTITHROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643768.

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The inactivation of human factor XIa by human antithrombin III (AT III) was studied under pseudo-first order reaction conditions (excess AT III) both in the absence and presence of heparin. The time course of inhibition was followed using SDS-PAGE. After electrophoresis proteins were blotted onto nitrocellulose and stained either for glycoprotein or for AT III using antibodies against AT III. Concomittant with factor XIa inactivation two new slower migrating bands became visible on the blots. One of these, representing the intermediate complex consisting of one AT III complexed with one of the active sites present in factor XIa, appeared as a transient band. Complete inactivation resulted in a single band representing the complex of factor XIa with two AT III molecules. This indicates that inhibition of factor XIa by AT III can be described as:Quantitative analysis of the time course of inactivation was accomplished by measurement of the disappearance of factor XIa amidolytic activity towards the chromogenic substrate S2366. Pseudo first order reaction kinetics were observed throughout. The time course of inactivation and the distribution of the reaction products observed upon gelelectrophoresis are best explained assuming a mechanism of inactivation in which the two active sites present in factor XIa are inhibited in random order (i.e. independent of each other) with the same rate constant of inhibition (k1= k2)- The rate constant of inactivation for the active sites in factor XIa was found to be 1,000 M-1 s-1 in the absence of heparin and 34,900 M-1 s-1 in the presence of saturating amounts of heparin.- From the kinetic data a binding constant Kd of 0.11 uM was inferred for the binding of AT III to heparin. Experiments with four well characterized heparin fractions indicate, that the actual magnitude of the rate enhancement of factor XIa inactivation is, however, not only due to the binding of AT III to heparin, but also depends on the type of heparin to which the AT III is bound.
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Goto, T., D. Kudo, R. Uchimido, K. Yamakawa, M. Hayakawa, S. Kushimoto, and H. Yasunaga. "Sepsis Phenotypes and the Effect of Antithrombin III." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a6006.

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Schwartz, R., E. Kavanagh, K. Bauer, R. Rosenberg, J. Ballard, J. Latino, V. Strother, M. Mosesson, W. Haire, and M. DeLeo. "ANTITHROMBIN III CONCENTRATE (AT-III) FOR PROPHYLAXIS ANDTREATMENT OF CONGENITAL AND ACQUIREDAT-III DEFCIENCY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643678.

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An investigation has been undertakenin 13 patient studies to determine the efficacy of AT-III in prevention and treatment of thrombosis in patients with congenital (cong.) and acquired (acq.) AT-III deficiency. The mean in vivo incremental recovery of 17 infusions of AT-III in 7 patientswith cong. AT-III deficiency (2 kinetic studies, 5 prophylaxis) was 1.4%/U/kg (functional assay) administered. The mean in vivo recovery of 38 infusions in 4 non-bleeding patients(3 cong., 1 acq.) treated for thrombosis or pulmonary embolism (P.E.) with heparin was 1.33%/U/kg which was not significantly different. The half-life determined in an earlier study exceeded 2.5 days. All patients treated prophylactically or therapeutically received a loading dose to increase plasma AT-III to 120%, and then received maintenance doses, generally every 24 hours, to maintain plasma AT-III levels in the general range 80-120%. AT-III levels were monitored every 12 hours initially and doses and intervals modified accordingly. None of 5 patients with cong. deficiency treated prophylactically for high risk situations (surgery, delivery, catheterization) developed a thrombotic complication. Six patients (3 cong., 2 acq., 1 probably acq.) were treated for thrombosis/P.E., two of whom were pregnant. Heparin resistance was reversed in two, both pregnant. One patient with superior mesenteric-portal vein thrombosis (cong. deficiency) and another with superior mesenteric artery-aortic occlusion (acq. deficiency) survived without further progression of thrombosis. DIC resolved in one patient treated with AT-III and benefit was observed in a 2nd patient as well. AT-III was well tolerated, with but a single mild reaction in 176 infusions. We conclude AT-III may be beneficialas prophylaxis in patients with cong.AT-III deficiency during high thrombotic risk situations, as well as anadjunct to heparin in treatment for thrombotic complications in congenital and acquired AT-III deficiency.
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Stüber, W., H. Pelzer, and N. Heimburger. "INDUCTION OF ANTITHROMBIN III (AT III) ANTIBODIES BY IMMUNIZATION WITH SYNTHETIC PEPTIDES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644355.

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The primary structure of AT III was examined in respect of potential antigenic sites. The topics were the determination of the hydrophilicity, hydropathy, acrophilicity and the propensities for alpha-helices, B-turns and 13-sheets. The peptides AT III 21-34, 21-42, 129 - 140, 226 - 240 and 343 -363 were synthesized using the solid phase peptide synthesis methode. The subsequent purification of the crude peptides was achieved by h.p.I.e. or by ion exchange chromatography. The peptides were coupled to keyhole limpet hemocyanine (KLH) via thioether bonds. Antisera against KLH-peptides were raised in rabbits (n = 25) and tested with AT III-coated polystyrene tubes; bound antibodies were detected with anti-rabbit-IgG-peroxidase. Obtained antisera were further purified by immuno-adsorption using immobilized AT III. Polystyrene tubes were coated with purified peptide antibodies and binding of AT III was studied with enzyme immunoassay technique (EIA) using anti-AT III-peroxidase.As a result, immunoreactivity of rabbit antisera against synthetic peptides of AT III could be achieved. The obtained antibodies against the individual synthetic peptides as well as their mixtures exhibited specific binding to AT III when tested with EIA.
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