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 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Biophysics
- Molecular Biology
- Structural Biology
Cite this
}
Refolding and release of tubulins by a functional immobilized groEL column. / Phadtare, Sangita; Fisher, Mark T.; Yarbrough, Lynwood R.
In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1208, No. 1, 21.09.1994, p. 189-192.Research output: Contribution to journal › Article
TY - JOUR
T1 - Refolding and release of tubulins by a functional immobilized groEL column
AU - Phadtare, Sangita
AU - Fisher, Mark T.
AU - Yarbrough, Lynwood R.
PY - 1994/9/21
Y1 - 1994/9/21
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0028024362&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028024362&partnerID=8YFLogxK
U2 - 10.1016/0167-4838(94)90178-3
DO - 10.1016/0167-4838(94)90178-3
M3 - Article
C2 - 7916211
AN - SCOPUS:0028024362
VL - 1208
SP - 189
EP - 192
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
SN - 1570-9639
IS - 1
ER -