Dissociation of creatine kinase under different denaturation conditions.
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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Department of Biological Science and Biotechnology, School of Life Science and Engineering, Tsinghua University, Beijing, 100084, P. R. China.
Zhang
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Zhang
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Zhou
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D000818:Animals; D003402:Creatine Kinase / Q000737:chemistry* / Q000302:isolation & purification; D003432:Cross-Linking Reagents; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D018482:Muscle, Skeletal; D011489:Protein Denaturation; D011817:Rabbits; D013388:Succinimides; D014508:Urea
D003432:Cross-Linking Reagents; D013388:Succinimides; D014508:Urea; D003402:Creatine Kinase; C011240:dithiobis(succinimidylpropionate)