Academic literature on the topic 'Anti-Xa Assay'

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Journal articles on the topic "Anti-Xa Assay"

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Greene, Lindsey A., Connie Law, Mike Jung, Sara Walton, and Leslie J. Raffini. "Lack Of Anti-Xa Assay Standardization Results In Significant Dose Variation In Neonates and Children Receiving Enoxaparin." Blood 122, no. 21 (2013): 2379. http://dx.doi.org/10.1182/blood.v122.21.2379.2379.

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Abstract Introduction Due to favorable pharmacokinetic properties, enoxaparin is the most frequently used anticoagulant in children. Unlike adults, a developing hemostatic system provides rationale for therapeutic monitoring with an anti-Xa goal of 0.5-1 units/ml. However, accepted therapeutic ranges are not well correlated with clinical outcomes (i.e. thrombosis or hemorrhage) and there is no assay standardization. In 2011 the coagulation laboratory at the Children's Hospital of Philadelphia (CHOP) changed anti-Xa laboratory assays resulting in anti-Xa levels that were on average, 33% higher
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Billoir, Paul, Virginie Barbay, Luc Marie Joly, Marielle Fresel, Marie Hélène Chrétien, and Véronique Le Cam Duchez. "Anti-Xa Oral Anticoagulant Plasma Concentration Assay in Real Life: Rivaroxaban and Apixaban Quantification in Emergency With LMWH Calibrator." Annals of Pharmacotherapy 53, no. 4 (2018): 341–47. http://dx.doi.org/10.1177/1060028018811657.

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Background: Oral anti-Xa inhibitors have demonstrated noninferiority to vitamin K antagonists (VKAs) for the prevention of stroke in patients with atrial fibrillation and recurrent venous thromboembolism. They are associated with a decrease in major bleeding. In contrast with VKA, no coagulation monitoring is required. However, in clinical practice, determination of drug concentration is sometimes necessary. Objective: The objective of this study was to evaluate a low-molecular-weight heparin (LMWH) calibrated anti-Xa assay for the quantification of rivaroxaban and apixaban plasma concentratio
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Iampietro, R., A. M. Woolley, F. E. Preston, and S. Kitchen. "Anti Xa Monitoring during Treatment with Low Molecular Weight Heparin or Danaparoid: Inter-assay Variability." Thrombosis and Haemostasis 82, no. 10 (1999): 1289–93. http://dx.doi.org/10.1055/s-0037-1614377.

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SummaryIf laboratory monitoring of low molecular weight heparin (LMWH) therapy is required the test of choice is the anti Xa activity assay. The relationship between anti Xa results obtained using different techniques is unknown. The aim of the present study was to compare anti Xa results obtained with eight different commercially available anti Xa activity assays (five chromogenic and three clotting based assays) in samples from patients receiving either therapeutic or prophylactic LMWH (enoxaparin or dalteparin) or danaparoid.We have demonstrated that highly significant differences exist bet
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Siddiqui, Fakiha, Debra Hoppensteadt, Walter Jeske, Omer Iqbal, Alfonso Tafur, and Jawed Fareed. "Factor Xa Inhibitory Profile of Apixaban, Betrixaban, Edoxaban, and Rivaroxaban Does Not Fully Reflect Their Biologic Spectrum." Clinical and Applied Thrombosis/Hemostasis 25 (January 1, 2019): 107602961984752. http://dx.doi.org/10.1177/1076029619847524.

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The currently available oral anti-Xa agents are claimed to produce their anticoagulant and antithrombotic effects solely by the inhibition of factor Xa. This study profiled various anti-Xa drugs in routinely used laboratory assays to demonstrate that their effects are not solely related to the anti-Xa activities. Apixaban, betrixaban, edoxaban, and rivaroxaban were obtained commercially. Native and citrated whole blood was used for the activated clotting time (ACT) and thromboelastography (TEG). Citrated plasma was used for monitoring the prothrombin time (PT), activated partial thromboplastin
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Wang, Zhaoqing, Charles Frost, Andrew Shenker, and Yu Chen Barrett. "Clinical laboratory measurement of direct factor Xa inhibitors: Anti-Xa assay is preferable to prothrombin time assay." Thrombosis and Haemostasis 104, no. 12 (2010): 1263–71. http://dx.doi.org/10.1160/th10-05-0328.

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SummaryApixaban and other factor Xa (FXa) inhibitors are in late-stage clinical development for prevention and treatment of thromboembolic diseases. Although routine monitoring will not be required, in certain situations assessment of drug level may be helpful. This study evaluated the suitability of commercially available prothrombin time/international normalised ratio (PT/INR) and anti-FXa activity assays to measure FXa inhibitors in plasma. Twelve PT (ISI 0.89ﺹ1.88) and three anti-Xa assays were evaluated in vitro using human plasma spiked with four FXa inhibitors (0ﺹ2,000 ng/ml). Assay var
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Bessekaar, A. M. H. P. van den, J. Meeuwisse-Braun, and R. M. Bertina. "Monitoring Heparin Therapy: Relationships between the Activated Partial Thromboplastin Time and Heparin Assays Based on Ex-Vivo Heparin Samples." Thrombosis and Haemostasis 63, no. 01 (1990): 016–23. http://dx.doi.org/10.1055/s-0038-1645678.

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SummaryFive different APTT reagents, two amidolytic anti-ITa assays, one amidoiytic anti-Xa assay, and one coagulometric anti-Xa/ anti-IIa assay were used to assess the effect of heparin in patients treated for venous thromboembolic disease. Good correlations were observed between lug-transformed APYE> determined with the various reagents (correlation coefficients: 0.92-0.96).Nevertheless there were important differences in the slopes of the lines of relationship between the APTT reagents.Good correlations were observed between the anti-Xa and anti-IIa assay results (correlation coefficient
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Vera-Aguilera, Jesus, Hindi Yousef, Diego Beltran-Melgarejo, et al. "Clinical Scenarios for Discordant Anti-Xa." Advances in Hematology 2016 (2016): 1–6. http://dx.doi.org/10.1155/2016/4054806.

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Anti-Xa testmeasuresthe activity ofheparinagainst the activity of activated coagulation factor X; significant variability of anti-Xa levels in common clinical scenarios has been observed.Objective. To review the most common clinical settings in which anti-Xa results can be bias.Evidence Review. Guidelines and current literature search: we used PubMed, Medline, Embase, and MEDION, from 2000 to October 2013.Results. Anti-Xa test is widely used; however the assay underestimates heparin concentration in the presence of significant AT deficiency, pregnancy, end stage renal disease, and postthrombol
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Gilbert, M., V. Goret, N. Rolland, M. Samama, and F. Depasse. "Anti-Xa Monitoring: Inter-assay Variability." Thrombosis and Haemostasis 84, no. 12 (2000): 1122–23. http://dx.doi.org/10.1055/s-0037-1614183.

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Gilbert, M., V. Goret, N. Rolland, M. Samama, and F. Depasse. "Anti-Xa Monitoring: Inter-assay Variability." Thrombosis and Haemostasis 84, no. 12 (2000): 1122–23. http://dx.doi.org/10.1055/s-0037-1614184.

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Barrowcliffe, T. W., A. D. Curtis, T. P. Tomlinson, A. R. Hubbard, E. A. Johnson, and D. P. Thomas. "Standardization of Low Molecular Weight Heparins : A Collaborative Study." Thrombosis and Haemostasis 54, no. 03 (1985): 675–79. http://dx.doi.org/10.1055/s-0038-1660095.

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SummaryA collaborative study was carried out, in which eight laboratories each assayed eight low molecular weight (LMW) heparins against the International Standard (IS) for heparin. APTT assays and three types of anti-Xa method were used. The results of this study showed that:1. LMW heparins cannot be validly assayed against the IS by APTT or anti-Xa methods.2. Potencies of LMW heparins vs. the IS differed considerably between the four types of assay method used and also between different laboratories using the same type of method.3. Adoption of a single LMW heparin standard would improve vali
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Books on the topic "Anti-Xa Assay"

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Giudice, Mirella. Validation of an unfractionated heparin nomogram using an anti-factor Xa chromogenic assay. 1999.

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Book chapters on the topic "Anti-Xa Assay"

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Newall, Fiona. "Anti-factor Xa (Anti-Xa) Assay." In Haemostasis. Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-339-8_19.

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Dean, Christina L. "An Overview of Heparin Monitoring with the Anti-Xa Assay." In Methods in Molecular Biology. Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3175-1_22.

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Conference papers on the topic "Anti-Xa Assay"

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ten Cate, H., Ch P. HENNY, A. Sturk, A. Prins, and J. W. ten Cate. "COMPARATIVE INVESTIGATION OF CLOTTING AND CHROMOGENIC ASSAYS FOR HEPARIN AND LOW MOLECULAR WEIGHT HEPARIN-(OID) IN PLASMA OF VOLUNTEERS AND PATIENTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644166.

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Two recently developed and simplified anti-Xa methods, a chromogenic assay and a clot-based assay (Heptest) were investigated on their accuracy and ex-vivo characteristics. The coefficients of variation (c.v.) for heparin, a heparin fragment (K 2165) and a LMW hepa-rinoid (Org 10172) were respectively: Heptest, within assay c.v.: 5.4; 4.5; 5.0 % between-assay c.v.: 7.8; 5.8; 9.5 %. Chromogenic Anti-Xa assay, within assay c.v.: 3.7; 5.6; 4.6 %, between assay c.v.: 6.6; 8.2; 12.1 %. In plasma samples obtained from volunteers and patients who participated in clinical studies using heparin, K 2165
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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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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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Mammen, E. F., A. M. Farag, R. J. Sachs та J. M. Brown. "ANTITHROMBIN III, PLASMINOGEN, α2 ANTIPLASMIN, PREKALLIKREIN AND HEPARIN ASSAYS ON AN AUTOMATED COAGULATION LABORATORY (ACL 810) ANALYZER". У XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643254.

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A recently introduced automated, microcomputer controlled centrifugal analyzer ACL 810 (Instrumentation Laboratories, IL) performs both clot based and chromogenic substrate based assays. We compared the performance characteristics of this new instrument with the Multistat III Centrifugal Analyzer (MCA, Instrumentation Laboratories) and the Protopath system (American Dade). Antithrombin III (AT) and plasminogen (PLG) were assayed on the ACL 810 using II kits, on the MCA using Kabi kits, S-2238 and S-2251, and on the protopath Dade reagents. 02 Antiplasmin (AP) was determined on the ACL with kit
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Racanelli, A., and J. Fareed. "DIFFERENTIAL NEUTRALIZATION OF UNFRACTIONATED HEPARIN (UH) AND LOW MOLECULAR WEIGHT HEPARINS (LMWHS) BY HUMAN PLATELET FACTOR FOUR (PF-4)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643502.

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Platelet factor 4 neutralization profiles of four newly developed LMWHs, PK 10169 (Pharmuka, Gennevilliers, France) CY 216 (Choay, Paris, France), KABI 2165 (KabiVitrum, Stockholm, Sweden), OP 2123 (Opocrin, Corlo Italy) and an unfractionated porcine mucosal heparin were studied utilizing amidolytic (anti-factor Xa, anti-factor Ila) and clot based (APTT, Heptest ) assays. The neutralization studies were carried out in normal human pooled plasma in two experimental protocolsIn one set of experiments, PF-4 (10μg/ml) was added to varying amounts of UH or LMWH (10-2.5 μg/ml). In the second set of
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Emanuele, R. M., J. C. Lormeau, J. Choay, and J. Fareed. "THE MOLECULAR WEIGHT DEPENDENT EFFECTS OF HEPARIN ON THROMBOPLASTIN ACTIVATED PROTEASES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644178.

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Five different molecular weight (M. W.) fractions of heparin (M. W.'s 23,000 ; 17,450 ; 13,300 ; 9,000 and 5,100) were prepared by gel-filtration. Screening of these fractions in global and amidolytic assaysat a concentration of 2.5 ug/ml revealed a dependence on M. W. for the potency response. In the APTT, TT, Heptest, amidolytic anti Xa and Ila assays, an increase in potency was observed with increasing M. W.. This relationship remained consistent to 13,300 M. W. after which no further increases in potency were observed. However, when the same fractions were screenedfor their effect on proth
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Giese, Ch, A. Knodler, R. Zimmermann, and J. Harenberg. "A NEW ONE STAGE CLOTTING ASSAY FOR HEPARIN AND LOW MOLECULAR WEIGHT HEPARINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644851.

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Heparin and its low molecular weight (LMW) derivatives are usually measured by chromogenic or fluorogenic synthetic substrate assays and by coagulation tests. Since the activated partial thromboplastin time (aPTT) and thrombin clotting time (TCT) are insensitive to LMW heparins, we report here of data obtained with heptest, a new one stage modification of the original heparin in plasma assay of Yin. The assay was compared with the antifactor Xa chromogenic substrate S2222 method, the TCT and aPTT tests in 100 patients receiving unfractionated pig intestinal mucosa heparin and 100 patients trea
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Tapon-Bretaudière, J., A. M. Fischer, C. Millien, and A. Bros. "HEPARIN COFACTOR II ASSAY : IMPORTANCE AND CONTROL OF THE NON-CONTAMINATION BY HEPARIN OF DERMATAN SULFATE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644348.

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A chromogenic substrate method for the determination of heparin cofactor II (HC II) in plasma, based on its anti Fc Ila activity, has been developped in our laboratory, using dermatan sulfate (D.S.) as activator. We observed that D.S. from porcine skin, which was claimed not to be contaminated by heparin, was sometimes contaminated, depending upon the batch used. Moreover, a classical treatment of D.S. by nitrous acid, that specifically degrades heparin-like glycosaminoglycans, is not always sufficient and in some cases, needs to be repeated. It is thus important to check the absence of hepari
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Boneu, B., G. Houin, M. Rostin, J. L. Montastructure, P. d’Azemar, and B. Bayrou. "INTER-INDIVIDUAL PHARMACOKINETIC VARIATIONS AFTER INTRAVENOUS (IV) AND SUBCUTANEOUS (SC) INJECTION OF CY 216 IN HEALTHY SUBJECTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643235.

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We investigated the pharmacokinetic parameters and their inter individual variations of a low molecular weight heparin (LMWH) derivative (CY 216, Fraxiparine R, Choay). In a cross-over study, 100 anti Xa IC u/kg were injected in 12 healthy volunteers, either by IV or SC route, at one week interval. The pharmacological effects were followed on 12 serial citrated samples for 24h: - anti factor Xa (AXa) activity (chromogenic assay calibrated against CY 216); - APTT and thrombin clotting time prolongation. The main pharmacokinetic parameters (elimination half-life (T|); clearance (cl); distributio
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Fischer, A. M., J. Tapon-Bretaudière, M. D. Dautzenberg, C. Sternberg, and J. Choay. "EVIDENCE FOR A HOMOLOGY BETWEEN THE HEPARIN AND HEPARAN SULFATE BINDING REGIONS TO ANTITHROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644360.

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As we have previously demonstrated, heparan sulfate, a glycosaminoglycan physiologically present on the endothelial wall, is, like heparin, unable to potentiate the inhibitory effect against Factors IIa and Xa of two abnormal type 3 antithrombin III (AT III) variants. We report here that a synthetic pentasaccharide which constitutes the sequence of the heparin binding site to AT III is also unable to potentiate these two AT III variants in an anti-Factor Xa assay. According to these data, we speculated the existence of a homology between the heparin and heparan sulfate binding regions to norma
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