Refolding and release of tubulins by a functional immobilized groEL column

Denatured tubulins form stable complexes with groEL upon dilution into refolding buffer. These complexes are retained on an immunoaffinity column which contains chemically immobilized antibodies to groEL. Tubulin remains bound to the immobilized groEL column after extensive washing and is released u...

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Bibliographic Details
Published in:	Biochimica et biophysica acta Vol. 1208; no. 1; p. 189
Main Authors:	Phadtare, S, Fisher, M T, Yarbrough, L R
Format:	Journal Article
Language:	English
Published:	Netherlands 21-09-1994
Subjects:	Adenosine Triphosphate - pharmacology Animals Bacterial Proteins Chaperonin 10 Chaperonin 60 Chickens Chromatography, Affinity Cricetinae Escherichia coli - genetics Heat-Shock Proteins - pharmacology Immunologic Techniques Protein Folding Recombinant Proteins - isolation & purification Tubulin - chemistry Tubulin - genetics Tubulin - metabolism
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Summary:	Denatured tubulins form stable complexes with groEL upon dilution into refolding buffer. These complexes are retained on an immunoaffinity column which contains chemically immobilized antibodies to groEL. Tubulin remains bound to the immobilized groEL column 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.
ISSN:	0006-3002
DOI:	10.1016/0167-4838(94)90178-3