| Autor: |
Morozova AV; Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia. avmoro@gmail.com, Khaitlina SY, Malinin AY |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry. Biokhimiia [Biochemistry (Mosc)] 2011 Apr; Vol. 76 (4), pp. 455-61. |
| DOI: |
10.1134/s0006297911040080 |
| Abstrakt: |
It has been found that actin-specific bacterial protease ECP32 cleaves prokaryotic heat shock protein DnaK, which belongs to the family of heat shock proteins with molecular weight 70 kDa. We propose a new one-step method for DnaK purification using heat treatment. The technique yields ~1 mg of partially purified DnaK from 25 g of wet bacterial biomass. Polyclonal antibodies against DnaK were obtained. The degree of ECP32 catalyzed proteolysis of partially purified DnaK and that of DnaK in initial cell extracts was compared. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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