Title data
Rosin-Arbesfeld, Rina ; Mashia, Pnina ; Willbold, Dieter ; Rösch, Paul ; Tronick, Steven R. ; Yaniv, Abraham ; Gazit, Arnona:
Biological activity and intracellular location of the Tat protein of equine infectious anemia virus.
In: Gene.
Vol. 150
(1994)
Issue 2
.
- pp. 307-311.
ISSN 1879-0038
DOI: https://doi.org/10.1016/0378-1119(94)90443-X
Abstract in another language
The Tat protein of equine infectious anemia virus (EIAV) was synthesized in Escherichia coli using the inducible expression plasmid, pET16b, which contains a His.Tag leader, thus allowing for rapid and efficient enrichment of the histidine-tagged protein by metal affinity chromatography. Yields of up to 20 mg of Tat were obtained from 10” bacterial cells. The recombinant Tat protein was shown to potently trans-activate the EIAV long terminal repeat (LTR) following its introduction into canine cells by ‘scrape loading’. The EIAV Tat protein was found to localize predominantly within the cytoplasm, in contrast to HIV-l Tat. The availability of large amounts of purified functional EIAV Tat protein should greatly facilitate detailed structure-function analyses.
Further data
Item Type: | Article in a journal |
---|---|
Refereed: | Yes |
Institutions of the University: | Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Chair Biopolymers - Univ.-Prof. Dr. Paul Rösch Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry |
Result of work at the UBT: | Yes |
DDC Subjects: | 500 Science > 540 Chemistry 500 Science > 570 Life sciences, biology |
Date Deposited: | 10 Jan 2019 10:31 |
Last Modified: | 16 May 2019 05:37 |
URI: | https://eref.uni-bayreuth.de/id/eprint/46844 |