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  • Basic biochemical properties such as Michaelis constant (KM) and turnover number (kcat) of enzyme enteropeptidase was measured by electrochemical impedance spectroscopy. Both values determined by impedance measurements are in good agreement with those obtained by traditional spectroscopic techniques. Therefore one can suppose that electrochemical methods might be successful for such measurements also in the case where usual ones (UV-Vis, fluorescence spectroscopy) are not able to determine these enzyme characteristics.
  • Basic biochemical properties such as Michaelis constant (KM) and turnover number (kcat) of enzyme enteropeptidase was measured by electrochemical impedance spectroscopy. Both values determined by impedance measurements are in good agreement with those obtained by traditional spectroscopic techniques. Therefore one can suppose that electrochemical methods might be successful for such measurements also in the case where usual ones (UV-Vis, fluorescence spectroscopy) are not able to determine these enzyme characteristics. (en)
Title
  • Electrochemistry as a Tool for an Enzyme Characterization
  • Electrochemistry as a Tool for an Enzyme Characterization (en)
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  • Electrochemistry as a Tool for an Enzyme Characterization
  • Electrochemistry as a Tool for an Enzyme Characterization (en)
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  • RIV/61388955:_____/14:00428758!RIV15-AV0-61388955
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  • RIV/61388955:_____/14:00428758
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  • electrochemistry; Enterokinase; Impedance spectroscopy (en)
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  • Sborník přednášek mezinárodní odborné konference XXXIV. Moderní Elektrochemické Metody
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  • Híveš, J.
  • Sokolová, Romana
  • Gál, M.
  • Jiríčková, K.
  • Krahulec, J.
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  • 978-80-905221-2-1
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