Modern bioanalysis of proteins by electrophoretic techniques

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00064203%3A_____%2F14%3A10294011" target="_blank" >RIV/00064203:_____/14:10294011 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11130/14:10294011
Result on the web
<a href="http://dx.doi.org/10.1007/978-1-62703-977-2_28" target="_blank" >http://dx.doi.org/10.1007/978-1-62703-977-2_28</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/978-1-62703-977-2_28" target="_blank" >10.1007/978-1-62703-977-2_28</a>

Result language
angličtina
Original language name
Modern bioanalysis of proteins by electrophoretic techniques
Original language 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 animalspecies, 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 ?L. Sodiumborate 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 ?m and electric field intensity of 350 V/cm. Optimal detection wavelength
Czech name
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Czech description
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Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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