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      A simple and selective liquid chromatography- tandem mass spectrometry method for determination of ε-aminocaproic acid in human plasma

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      Journal of Applied Bioanalysis
      Betasciencepress Publishing

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          Abstract

          Understanding the clinical pharmacology of the antifibrinolytic drug epsilon-aminocaproic acid (EACA) is critical for rational drug administration in children. The aim of this study is to develop a reliable assay for the determination of EACA in human plasma. We describe a high-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) assay for EACA in human plasma. Sample preparation involved plasma dilution (1:2040), followed by reversed-phase chromatographic separation and selective detection using tandem mass spectrometry. EACA had a linear range of 1 - 250 μg/mL. The intraday precision based on the standard deviation of replicates of quality control samples ranged from 4.7 to 10.4% and the accuracy ranged from 92-106%. The interday precision ranged from 4.6 to 9.8% and the accuracy ranged from 95-103%. Stability studies showed that EACA was stable during the conditions for sample preparation and storage. The described method is robust and successfully employed for clinical studies of EACA in children.

          Most cited references23

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          Key elements of bioanalytical method validation for small molecules.

          Method validation is a process that demonstrates that a method will successfully meet or exceed the minimum standards recommended in the Food and Drug Administration (FDA) guidance for accuracy, precision, selectivity, sensitivity, reproducibility, and stability. This article discusses the validation of bioanalytical methods for small molecules with emphasis on chromatographic techniques. We present current thinking on validation requirements as described in the current FDA Guidance and subsequent 2006 Bioanalytical Methods Validation Workshop white paper.
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            Clinical pharmacology of aminocaproic and tranexamic acids.

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              Regulation of fibrinolysis by C-terminal lysines operates through plasminogen and plasmin but not tissue-type plasminogen activator.

              Binding of tissue-type plasminogen (Pgn) activator (t-PA) and Pgn to fibrin regulates plasmin generation, but there is no consistent, quantitative understanding of the individual contribution of t-PA finger and kringle 2 domains to the regulation of fibrinolysis. Kringle domains bind to lysines in fibrin, and this interaction can be studied by competition with lysine analogs and removal of C-terminal lysines by carboxypeptidase B (CPB).
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                Author and article information

                Journal
                Journal of Applied Bioanalysis
                J Appl Bioanal
                Betasciencepress Publishing
                2405710X
                July 15 2015
                July 15 2015
                : 1
                : 3
                : 99-107
                Article
                10.17145/jab.15.016
                ce564442-b7fe-4859-b180-3bf29edd5467
                © 2015

                This work is licensed under a Creative Commons Attribution 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by/3.0/

                History

                General life sciences,Chemistry,Analytical chemistry,Life sciences
                General life sciences, Chemistry, Analytical chemistry, Life sciences

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