Dissociation of Creatine Kinase under Different Denaturation Conditions

B. He^1,3, Y. Zhang^1,4, T. Zhang¹, and H.-M. Zhou^1,2*

¹Department of Biological Science and Biotechnology, School of Life Science and Engineering, Tsinghua University, Beijing, 100084 P. R. China; fax: (8610) 62785505; E-mail: zhm-dbs@tsinghua.edu.cn

²National Laboratory of Macromolecules, Institute of Biophysics, Academia Sinica, Beijing, 100101 P. R. China

³Present address: 388 Dillard, 326A P.O. Box 615, Station No. 2, Charlottesville, VA, 22904 USA

⁴Present address: 600 Fairchild Center, Department of Biological Sciences, Columbia University, New York, N. Y., 10027 USA

^* To whom correspondence should be addressed.

Received January 19, 1998

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Dissociation of dimeric creatine kinase under different denaturation conditions was investigated using the cleavable cross-linker 3,3´-dithiobis(succinimidyl propionate). The results show that at low denaturant concentrations or at low denaturation temperatures the creatine kinase was mostly inactivated, but the enzyme was still either in the dimeric state or very slightly dissociated. It appears, therefore, that for several denaturation conditions, inactivation of the enzyme is not due to the dissociation of the active dimer.

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KEY WORDS: creatine kinase, cross-linking, dissociation, urea

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