Refolding and release of tubulins by a functional immobilized groEL column

Sangita Phadtare, Mark T. Fisher, Lynwood R. Yarbrough

Research output: Contribution to journalArticle

25 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)189-192
Number of pages4
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1208
Issue number1
DOIs
StatePublished - Sep 21 1994
Externally publishedYes

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Tubulin
Immobilized Antibodies
Glutamate-Ammonia Ligase
Washing
Dilution
Buffers
Adenosine Triphosphate

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

Cite this

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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 journalArticle

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