Modern Bioanalysis of Proteins by Electrophoretic Techniques

C 2014

Modern Bioanalysis of Proteins by Electrophoretic Techniques

KŘÍŽKOVÁ, Soňa, Markéta RYVOLOVÁ, Michal MASAŘÍK, Ondřej ZÍTKA, Vojtěch ADAM et. al.

Basic information

Original name

Modern Bioanalysis of Proteins by Electrophoretic Techniques

Authors

KŘÍŽKOVÁ, Soňa, Markéta RYVOLOVÁ, Michal MASAŘÍK, Ondřej ZÍTKA, Vojtěch ADAM, Jaromír HUBÁLEK, Tomas ECKSCHLAGER and René KIZEK

Edition

New York, Protein Downstream Processing, p. 381-396, 16 pp. Methods in Molecular Biology, Vol. 1129, 2014

Publisher

Springer

Other information

Language

English

Type of outcome

Kapitola resp. kapitoly v odborné knize

Field of Study

Genetics and molecular biology

Confidentiality degree

není předmětem státního či obchodního tajemství

Publication form

electronic version available online

Organization unit

Faculty of Medicine

ISBN

978-1-62703-976-5

DOI

http://dx.doi.org/10.1007/978-1-62703-977-2_28

Keywords in English

Metallomics; Gel electrophoresis; Capillary electrophoresis; Chip electrophoresis;18 Electrochemistry

Abstract

V originále

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 center 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 \iL. 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 um and electric field intensity of 350 V/cm. Optimal detection wavelength was 254 nm.

Citovat

KŘÍŽKOVÁ, Soňa, Markéta RYVOLOVÁ, Michal MASAŘÍK, Ondřej ZÍTKA, Vojtěch ADAM, Jaromír HUBÁLEK, Tomas ECKSCHLAGER and René KIZEK. Modern Bioanalysis of Proteins by Electrophoretic Techniques. Online. In Nikolaos Labrou. Protein Downstream Processing. New York: Springer, 2014, p. 381-396. Methods in Molecular Biology, Vol. 1129. ISBN 978-1-62703-976-5. Available from: https://dx.doi.org/10.1007/978-1-62703-977-2_28.

@inbook{1187248,
   author = {Křížková, Soňa and Ryvolová, Markéta and Masařík, Michal and Zítka, Ondřej and Adam, Vojtěch and Hubálek, Jaromír and Eckschlager, Tomas and Kizek, René},
   address = {New York},
   booktitle = {Protein Downstream Processing},
   doi = {http://dx.doi.org/10.1007/978-1-62703-977-2_28},
   editor = {Nikolaos Labrou},
   keywords = {Metallomics; Gel electrophoresis; Capillary electrophoresis; Chip electrophoresis;18 Electrochemistry},
   howpublished = {elektronická verze "online"},
   language = {eng},
   location = {New York},
   isbn = {978-1-62703-976-5},
   pages = {381-396},
   publisher = {Springer},
   title = {Modern Bioanalysis of Proteins by Electrophoretic Techniques},
   year = {2014}
}

TY  - CHAP
ID  - 1187248
AU  - Křížková, Soňa - Ryvolová, Markéta - Masařík, Michal - Zítka, Ondřej - Adam, Vojtěch - Hubálek, Jaromír - Eckschlager, Tomas - Kizek, René
PY  - 2014
TI  - Modern Bioanalysis of Proteins by Electrophoretic Techniques
VL  - Methods in Molecular Biology, Vol. 1129
PB  - Springer
CY  - New York
SN  - 9781627039765
KW  - Metallomics
KW  - Gel electrophoresis
KW  - Capillary electrophoresis
KW  - Chip electrophoresis;18 Electrochemistry
N2  - 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 center 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 \iL. 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 um and electric field intensity of 350 V/cm. Optimal detection wavelength was 254 nm.
ER  -

KŘÍŽKOVÁ, Soňa, Markéta RYVOLOVÁ, Michal MASAŘÍK, Ondřej ZÍTKA, Vojtěch ADAM, Jaromír HUBÁLEK, Tomas ECKSCHLAGER and René KIZEK. Modern Bioanalysis of Proteins by Electrophoretic Techniques. Online. In Nikolaos Labrou. \textit{Protein Downstream Processing}. New York: Springer, 2014, p.~381-396. Methods in Molecular Biology, Vol. 1129. ISBN~978-1-62703-976-5. Available from: https://dx.doi.org/10.1007/978-1-62703-977-2\_{}28.

Detailed Information on Publication Record