PMID:7904492

Citation	Khandekar, SS, Bettencourt, BM, Kelley, KC and Recny, MA (1993) A simple and rapid method for the purification of GroEL, an Escherichia coli homolog of the heat shock protein 60 family of molecular chaperonins. Protein Expr. Purif. 4:580-4
Abstract	GroEL, an Escherichia coli homolog of the heat shock protein 60 family of molecular chaperonins, has been implicated as a target of T cell-mediated immune responses in a broad spectrum of infections. In order to produce large quantities of native protein for raising and stimulating GroEL specific T cell lines, we have developed a simple and rapid two-step protocol for purifying native E. coli GroEL heat shock (or stress) protein which takes advantage of the inherent structural and functional properties of the protein. Based on a combination of gel exclusion chromatography, ATPase activity assay, isoelectric focusing, and circular dichroism analyses we conclude that our purification process yields native tetradecameric GroEL.
Links	PubMed Online version:10.1006/prep.1993.1076
Keywords	Adenosine Triphosphate/metabolism; Bacterial Proteins/isolation & purification; Chaperonin 60; Circular Dichroism; Escherichia coli/chemistry; Heat-Shock Proteins/isolation & purification; Isoelectric Focusing; Molecular Weight; Protein Conformation; Spectrophotometry, Ultraviolet
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