title: Equilibrium intermediates in the unfolding pathway of creatine kinase.
abstract: The unfolding of creatine kinase in various concentrations of guanidine hydrochloride of increasing concentrations has been investigated by combination of size-exclusion chromatography (SEC) with other methods. There are two peaks in the profiles of SEC in GuHCl at moderate concentrations, showing that unfolding of creatine kinase goes through dimeric and monomeric intermediates with increasing guanidine hydrochloride concentrations. Both intermediates have relatively compact structure and retain considerable ordered structure.
authors.affiliation: National Laboratory of Biomacromolecules, Academia Sinica, Beijing, China.
authors.forename: Y L
authors.initials: YL
authors.lastname: Zhang
authors.forename: Y X
authors.initials: YX
authors.lastname: Fan
authors.forename: G C
authors.initials: GC
authors.lastname: Huang
authors.forename: J X
authors.initials: JX
authors.lastname: Zhou
authors.forename: J M
authors.initials: JM
authors.lastname: Zhou
mesh_terms: D002850:Chromatography, Gel; D003402:Creatine Kinase / Q000737:chemistry* / Q000187:drug effects; D019791:Guanidine / Q000494:pharmacology; D011487:Protein Conformation; D011489:Protein Denaturation
chemical_list: D003402:Creatine Kinase; D019791:Guanidine