title: Inactivation of creatine kinase is due to the conformational changes of the active sites during thermal denaturation.
abstract: The conformational changes of the active site of creatine kinase (ATP: creatine N-phosphotransferase EC 2.7.3.2.) during thermal denaturation was followed by changes in fluorescence at the active site of the enzyme labeled by o-phthalaldehyde. Conformational changes of the active site occurred at the same time as inactivation of the enzyme. The active site changes occurred before the denaturation of the enzyme molecule as a whole was detected. The above results showed that the thermal inactivation of the creatine kinase was due to the conformational changes of its active sites.
authors.affiliation: Department of Biological Science and Biotechnology, Tsinghua University, Beijing, P.R.China.
authors.forename: J H
authors.initials: JH
authors.lastname: Bai
authors.forename: S Y
authors.initials: SY
authors.lastname: Zheng
authors.forename: H M
authors.initials: HM
authors.lastname: Zhou
mesh_terms: D001665:Binding Sites; D003402:Creatine Kinase / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D019281:Dimerization; D006358:Hot Temperature; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013050:Spectrometry, Fluorescence; D009764:o-Phthalaldehyde
chemical_list: D009764:o-Phthalaldehyde; D003402:Creatine Kinase