REFOLDING AND RELEASE OF TUBULINS BY A FUNCTIONAL IMMOBILIZED GROEL COLUMN

Authors
PHADTARE S FISHER MT YARBROUGH LR
Citation
S. Phadtare et al., REFOLDING AND RELEASE OF TUBULINS BY A FUNCTIONAL IMMOBILIZED GROEL COLUMN, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1208(1), 1994, pp. 189-192
Citations number
19
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta. Protein structure and molecular enzymology → ACNP
ISSN journal
01674838
Volume
1208
Issue
1
Year of publication
1994
Pages
189 - 192
Database
ISI
SICI code
0167-4838(1994)1208:1<189:RAROTB>2.0.ZU;2-G
Abstract
Denatured tubulins form stable complexes with groEL upon dilution into refolding buffer. These complexes are retained on an immunoaffinity c olumn which contains chemically immobilized antibodies to groEL. Tubul in remains bound to the immobilized groEL column after extensive washi ng and is released upon incubation with groES and ATP. Similar results were obtained with glutamine synthetase. These data suggest that groE L can function while it is attached to a solid support system.