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Statements

Subject Item
n2:RIV%2F00216208%3A11130%2F14%3A10294011%21RIV15-MSM-11130___
rdf:type
n19:Vysledek skos:Concept
rdfs:seeAlso
http://dx.doi.org/10.1007/978-1-62703-977-2_28
dcterms:description
In 1957, protein rich in cysteine able to bind cadmium was isolated from horse kidney and named as metallothionein according to its structural properties. Further, this protein and metallothionein-like proteins have been found in tissues of other animal species, yeasts, fungi and plants. MT is as a potential cancer marker in the focus of interest, and its properties, functions, and behavior under various conditions are intensively studied. Our protocol describes separation of two major mammalian isoforms of MT (MT-1 and MT-2) using capillary electrophoresis (CE) coupled with UV detector. This protocol enables separation of MT isoforms and studying of their basic behavior as well as their quantification with detection limit in units of ng per μL. Sodium borate buffer (20 mM, pH 9.5) was optimized as a background electrolyte, and the separation was carried out in fused silica capillary with internal diameter of 75 μm and electric field intensity of 350 V/cm. Optimal detection wavelength was 254 nm. In 1957, protein rich in cysteine able to bind cadmium was isolated from horse kidney and named as metallothionein according to its structural properties. Further, this protein and metallothionein-like proteins have been found in tissues of other animal species, yeasts, fungi and plants. MT is as a potential cancer marker in the focus of interest, and its properties, functions, and behavior under various conditions are intensively studied. Our protocol describes separation of two major mammalian isoforms of MT (MT-1 and MT-2) using capillary electrophoresis (CE) coupled with UV detector. This protocol enables separation of MT isoforms and studying of their basic behavior as well as their quantification with detection limit in units of ng per μL. Sodium borate buffer (20 mM, pH 9.5) was optimized as a background electrolyte, and the separation was carried out in fused silica capillary with internal diameter of 75 μm and electric field intensity of 350 V/cm. Optimal detection wavelength was 254 nm.
dcterms:title
Modern bioanalysis of proteins by electrophoretic techniques Modern bioanalysis of proteins by electrophoretic techniques
skos:prefLabel
Modern bioanalysis of proteins by electrophoretic techniques Modern bioanalysis of proteins by electrophoretic techniques
skos:notation
RIV/00216208:11130/14:10294011!RIV15-MSM-11130___
n3:aktivita
n15:V
n3:aktivity
V
n3:dodaniDat
n4:2015
n3:domaciTvurceVysledku
n12:9974687
n3:druhVysledku
n21:C
n3:duvernostUdaju
n11:S
n3:entitaPredkladatele
n16:predkladatel
n3:idSjednocenehoVysledku
30027
n3:idVysledku
RIV/00216208:11130/14:10294011
n3:jazykVysledku
n18:eng
n3:klicovaSlova
Electrochemistry; Chip electrophoresis; Capillary electrophoresis; Gel electrophoresis; Metallomics
n3:klicoveSlovo
n10:Chip%20electrophoresis n10:Metallomics n10:Capillary%20electrophoresis n10:Gel%20electrophoresis n10:Electrochemistry
n3:kontrolniKodProRIV
[AA22DC2AE7A9]
n3:mistoVydani
New York City
n3:nazevEdiceCisloSvazku
Methods in Molecular Biology, Vol. 1129
n3:nazevZdroje
Protein Downstream Processing
n3:obor
n20:FD
n3:pocetDomacichTvurcuVysledku
1
n3:pocetStranKnihy
555
n3:pocetTvurcuVysledku
8
n3:rokUplatneniVysledku
n4:2014
n3:tvurceVysledku
Eckschlager, Tomáš Zítka, Ondřej Hubálek, Jaromír Adam, Vojtěch Křížková, Soňa Masařík, Michal Kízek, René Ryvolová, Markéta
s:numberOfPages
16
n6:doi
10.1007/978-1-62703-977-2_28
n8:hasPublisher
Humana Press
n17:isbn
978-1-62703-976-5
n14:organizacniJednotka
11130