title: Reactivation and refolding of a partially folded creatine kinase modified by 5,5'-dithio-bis(2-nitrobenzoic acid).
abstract: Creatine kinase with its thiol groups modified by 5, 5'-dithio-bis(2-nitrobenzoic acid) has been shown to be partially folded in a monomeric state using fluorescence, circular dichroism, proteolysis, and size exclusion chromatography studies. In the presence of DTT, the partially folded modified creatine kinase can be reactivated and refolded following a biphasic course, suggesting the existence of a monomeric intermediate during the refolding of CK. The results provide evidence for our previously suggested model of the refolding pathway of urea-denatured creatine kinase.
authors.affiliation: Department of Biological Science and Biotechnology, School of Life Science and Engineering, Beijing, 100084, China.
authors.forename: Y
authors.initials: Y
authors.lastname: Yang
authors.forename: Y D
authors.initials: YD
authors.lastname: Park
authors.forename: T W
authors.initials: TW
authors.lastname: Yu
authors.forename: H M
authors.initials: HM
authors.lastname: Zhou
mesh_terms: D000818:Animals; D002942:Circular Dichroism; D003402:Creatine Kinase / Q000737:chemistry*; D004228:Dithionitrobenzoic Acid / Q000494:pharmacology*; D004229:Dithiothreitol / Q000737:chemistry; D004789:Enzyme Activation; D007700:Kinetics; D018482:Muscle, Skeletal / Q000201:enzymology; D017510:Protein Folding; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D013438:Sulfhydryl Compounds / Q000737:chemistry
chemical_list: D013438:Sulfhydryl Compounds; D004228:Dithionitrobenzoic Acid; D003402:Creatine Kinase; D004229:Dithiothreitol