title: GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroEL.
abstract: The presence of GroEL/ES during the refolding of human carbonic anhydrase II (pseudo-wild type) was found to increase the yield of active enzyme from 65 to 100%. This chaperone action on the enzyme could be obtained by adding GroEL alone, and the time-course in that case was only moderately slower than the spontaneous process. Truncated forms of carbonic anhydrase, in which N-terminal helices were removed, also served as protein substrates for GroEL/ES. This demonstrates that N-terminally located helices are not obligatory as recognition motifs.
authors.affiliation: IFM-Department of Chemistry, Linköping University, Sweden.
authors.forename: M
authors.initials: M
authors.lastname: Persson
authors.forename: G
authors.initials: G
authors.lastname: Aronsson
authors.forename: N
authors.initials: N
authors.lastname: Bergenhem
authors.forename: P O
authors.initials: PO
authors.lastname: Freskgård
authors.forename: B H
authors.initials: BH
authors.lastname: Jonsson
authors.forename: B P
authors.initials: BP
authors.lastname: Surin
authors.forename: M D
authors.initials: MD
authors.lastname: Spangfort
authors.forename: U
authors.initials: U
authors.lastname: Carlsson
mesh_terms: D001665:Binding Sites; D002256:Carbonic Anhydrases / Q000737:chemistry*; D018835:Chaperonin 10 / Q000494:pharmacology*; D018834:Chaperonin 60 / Q000494:pharmacology*; D004793:Enzyme Reactivators / Q000494:pharmacology*; D006801:Humans; D017510:Protein Folding
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60; D004793:Enzyme Reactivators; D002256:Carbonic Anhydrases