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  • Matrix metalloproteinases (MMPs) represent a family of structurally related zinc-dependent metallopeptidases. MMPs are able to degrade both majority and minority components of extracellular matrix include the native helix of collagen. These enzymes take part in normal biological processes such as ontogenesis or wound healing but also in inflammatory, generative, and especially malign processes. Zinc ion plays structural and regulatory role in MMPs but it is mainly involved directly in the catalytic hydrolysis of protein substrates. The aim of this work was to propose and optimize the chronopotentiometric stripping analysis (CPSA) in connection with adsorptive transfer technique (AdTS) for MMP-9 detection. The method has been further employed to investigate MMP-9 interaction with collagen. Thanks to AdTS CPSA at hanging mercury drop electrode we were able to measure 5 ul sample volume. We optimized the following parameters: time of the accumulation of the sample on HMDE surface and the composition of
  • Matrix metalloproteinases (MMPs) represent a family of structurally related zinc-dependent metallopeptidases. MMPs are able to degrade both majority and minority components of extracellular matrix include the native helix of collagen. These enzymes take part in normal biological processes such as ontogenesis or wound healing but also in inflammatory, generative, and especially malign processes. Zinc ion plays structural and regulatory role in MMPs but it is mainly involved directly in the catalytic hydrolysis of protein substrates. The aim of this work was to propose and optimize the chronopotentiometric stripping analysis (CPSA) in connection with adsorptive transfer technique (AdTS) for MMP-9 detection. The method has been further employed to investigate MMP-9 interaction with collagen. Thanks to AdTS CPSA at hanging mercury drop electrode we were able to measure 5 ul sample volume. We optimized the following parameters: time of the accumulation of the sample on HMDE surface and the composition of (en)
  • Matrix metaloproteináz (MMPs) představují rodinu strukturně příbuzných zinek-závislé metallopeptidasi. MMPs jsou schopny degradovat větší či menší složky extracelulární matrice obsahují nativní helix kolagen. Tyto enzymy se účastní v běžných biologických procesech, jako jsou ontogeneze nebo hojení ran, ale také v zánětlivé, generativní, a zejména maligní procesy. Zinečnaté ionty hrají strukturální a regulační úlohu v MMPs, ale jsou zahrnuty hlavně přímo v katalytické hydrolýze bilkovýnných substrátů. Cílem této práce bylo navrhnout a optimalizovat chronopotenciometrickou analýzu (CPSA) v souvislosti s převodem adsorptive technika (AdTS) pro MMP-9 v obraze. Tato metoda byla dále využívána k prošetření MMP-9 interakce s kolagenem. Díky AdTS CPSA na visí kapka rtuti elektrody jsme byli schopni změřit objem 5 ml vzorku. My optimalizovány následující parametry: doba akumulace vzorku na povrch HMDE a složení podporující elektrolyt. Vhodná akumulační doba byla 90 s je pro oba MMP-9 a kolagenu a podporují (cs)
Title
  • An Investigation of interactions of matrix metalloproteinases with collagen by chronopotentiometric stripping analysis
  • An Investigation of interactions of matrix metalloproteinases with collagen by chronopotentiometric stripping analysis (en)
  • Studium interakci mezi matrixovými metaloproteinásami s kolagen pomocí chronopotenciometrie (cs)
skos:prefLabel
  • An Investigation of interactions of matrix metalloproteinases with collagen by chronopotentiometric stripping analysis
  • An Investigation of interactions of matrix metalloproteinases with collagen by chronopotentiometric stripping analysis (en)
  • Studium interakci mezi matrixovými metaloproteinásami s kolagen pomocí chronopotenciometrie (cs)
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  • RIV/62156489:43210/08:00134121!RIV09-AV0-43210___
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  • P(IAA401990701)
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  • 355697
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  • RIV/62156489:43210/08:00134121
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  • metalloproteinases; electrochemistry (en)
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  • [A1B13DBBCBF1]
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  • Prague, Czech Republic
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  • 12th International Conference on Electroanalysis
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  • Adam, Vojtěch
  • Húska, Dalibor
  • Kizek, René
  • Masařík, Michal
  • Trnková, Libuše
  • Zítka, Ondřej
issn
  • 0009-2770
number of pages
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  • Czech Chemical Society
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  • 43210
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