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Statements

Subject Item
n2:RIV%2F62156489%3A43210%2F08%3A00134121%21RIV09-AV0-43210___
rdf:type
n15:Vysledek skos:Concept
dcterms:description
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 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
dcterms:title
An Investigation of interactions of matrix metalloproteinases with collagen by chronopotentiometric stripping analysis Studium interakci mezi matrixovými metaloproteinásami s kolagen pomocí chronopotenciometrie An Investigation of interactions of matrix metalloproteinases with collagen by chronopotentiometric stripping analysis
skos:prefLabel
An Investigation of interactions of matrix metalloproteinases with collagen by chronopotentiometric stripping analysis Studium interakci mezi matrixovými metaloproteinásami s kolagen pomocí chronopotenciometrie An Investigation of interactions of matrix metalloproteinases with collagen by chronopotentiometric stripping analysis
skos:notation
RIV/62156489:43210/08:00134121!RIV09-AV0-43210___
n3:aktivita
n11:P
n3:aktivity
P(IAA401990701)
n3:dodaniDat
n16:2009
n3:domaciTvurceVysledku
n6:9000240 n6:2307049 n6:8740658 n6:4995775 n6:3931315 n6:3790185
n3:druhVysledku
n5:D
n3:duvernostUdaju
n14:S
n3:entitaPredkladatele
n18:predkladatel
n3:idSjednocenehoVysledku
355697
n3:idVysledku
RIV/62156489:43210/08:00134121
n3:jazykVysledku
n7:eng
n3:klicovaSlova
metalloproteinases; electrochemistry
n3:klicoveSlovo
n4:electrochemistry n4:metalloproteinases
n3:kontrolniKodProRIV
[A1B13DBBCBF1]
n3:mistoVydani
Prague, Czech Republic
n3:nazevZdroje
12th International Conference on Electroanalysis
n3:obor
n19:CE
n3:pocetDomacichTvurcuVysledku
6
n3:pocetTvurcuVysledku
6
n3:projekt
n17:IAA401990701
n3:rokUplatneniVysledku
n16:2008
n3:tvurceVysledku
Adam, Vojtěch Trnková, Libuše Zítka, Ondřej Húska, Dalibor Masařík, Michal Kizek, René
s:issn
0009-2770
s:numberOfPages
1
n12:hasPublisher
Czech Chemical Society
n9:organizacniJednotka
43210