Comparison of classical and affinity purification techniques of Mason-Pfizer monkey virus capsid protein; the alteration of the product by an affinity tag.

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F01%3A00004739" target="_blank" >RIV/60461373:22330/01:00004739 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/01:57010133 RIV/60461373:22330/01:00006141
Result on the web
—
DOI - Digital Object Identifier
—

Result language
čeština
Original language name
Comparison of classical and affinity purification techniques of Mason-Pfizer monkey virus capsid protein; the alteration of the product by an affinity tag.
Original language description
Retroviral capsid protein was expressed in Escherichia coli i) as a wild type protein, ii) with histidine tag (CA6His), and iii) as a protein containing a C-terminal fusion to a viral protease cleavage site followed by a six-histidine tag (CA6aa6His). Wehave found that these C-terminal fusions dramatically influenced properties and morphology of structures formed by CA protein in E. coli. We showed that widely used histidine anchor may significantly alter properties of the protein of interest.
Czech name
Comparison of classical and affinity purification techniques of Mason-Pfizer monkey virus capsid protein; the alteration of the product by an affinity tag.
Czech description
—

Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2001
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)