Abstract
Denatured tubulins form stable complexes with groEL upon dilution into refolding buffer. These complexes are retained on an immunoaffmity column which contains chemically immobilized antibodies to groEL. Tubulin remains bound to the immobilized groEL colunm after extensive washing and is released upon incubation with groES and ATP. Similar results were obtained with glutamine synthetase. These data suggest that groEL can function while it is attached to a solid support system.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 189-192 |
| Number of pages | 4 |
| Journal | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
| Volume | 1208 |
| Issue number | 1 |
| DOIs | |
| State | Published - Sep 21 1994 |
All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
Fingerprint Dive into the research topics of 'Refolding and release of tubulins by a functional immobilized groEL column'. Together they form a unique fingerprint.
Cite this
Phadtare, S., Fisher, M. T., & Yarbrough, L. R. (1994). Refolding and release of tubulins by a functional immobilized groEL column. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 1208(1), 189-192. https://doi.org/10.1016/0167-4838(94)90178-3