| Autor: |
Shi, Jianguo, Lindsay, William P., Huckle, James W., Morby, Andrew P., Robinson, Nigel J. |
| Jazyk: |
angličtina |
| Předmět: |
|
| Zdroj: |
FEBS Letters. (2-3):159-163 |
| ISSN: |
0014-5793 |
| DOI: |
10.1016/0014-5793(92)80509-F |
| Popis: |
The recently isolated Synechococcus genesmtA encodes the only characterised prokaryotic protein designated to be a metallothionein (MT). To examine the metal-binding properties of its product thesmtA gene was expressed inEscherichia coli as a car☐yterminal extension of glutathione-S-transferase. The pH of half dissociation of Zn, Cd and Cu ions from the expressed protein was determined to be 4.10, 3.50, 2.35, respectively, indicating a high affinity for these ions (in particular for Zn in comparison to mammalian MT).E. coli expressing this gene showed enhanced (ca. 3-fold) accumulation of Zn. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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