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 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.
Phadtare
S
S
Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City 66160-7421.
Fisher
M T
MT
Yarbrough
L R
LR
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D002645:Chickens; D002846:Chromatography, Affinity; D006224:Cricetinae; D004926:Escherichia coli / Q000235:genetics; D006360:Heat-Shock Proteins / Q000494:pharmacology; D007158:Immunologic Techniques; D017510:Protein Folding; D011994:Recombinant Proteins / Q000302:isolation & purification; D014404:Tubulin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D011994:Recombinant Proteins; D014404:Tubulin; D000255:Adenosine Triphosphate