| Autor: |
Evers, Melchior E., Huhse, Bettina, Titorenko, Vladimir I., Kunau, Wolf H., Hartl, Franz-Ulrich, Harder, Wim, Veenhuis, Marten |
| Zdroj: |
FEBS Letters; April 1993, Vol. 321 Issue: 1 p32-36, 5p |
| Abstrakt: |
We used peroxisomal alcohol oxidase (AO) for the affinity purification of molecular chaperones from yeasts. Methodical studies showed that up to 0.8 mg of purified bacterial GroEL was able to bind per ml of immobilized denatured AO column material. Using crude extracts of Hansenula polymorphaor Saccharomyces cerevisiae, several proteins were specifically eluted with Mg‐ATP which were recognized by antibodies against hsp60 or hsp70. One H. polymorpha70 kDa protein was strongly induced during growth at elevated temperatures, whereas a second 70 kDa protein as well as a 60 kDa protein showed strong protein sequence homology to mitochondrial SSCI and hsp60, respectively, from S. cerevisiae. |
| Databáze: |
Supplemental Index |
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