CONFORMATIONAL AND ACTIVITY CHANGES OF HUMAN CREATINE KINASE DURING SDS DENATURATION
人肌肌酸激酶在SDS溶液中失活与构象变化的比较研究

The conformational changes of human creatine kinase during titration by Sodium Dodecyl Sulfate(SDS)solution were studied by ulhaviolet difference spectra ,intrin sic protein fluorescence and Circular Dicchrosm (CD). The adults showed that changes of conformation measured in abothance of 287nm, the red shift of fluorelnhaon maximaand the nUmbers of expend SH groups were much fasfor than that of activity.Changes in the fluormce emission spectla of the during Sac titration occur in tWO stagals.decade of emission intenSity took place at low Sac concentration with with shill of ion maxim,when the concentration of Sin reached tO 2. Innnol/L, the emission intensity fllrther changes in fluoascence propend occur at a more higher Sin contion.The CD special showed that the secondary strUctWh of enzyme in our expeconcentlation of Sin had no obvious change. The present results supports the condition that the conformational state of the active site of is very fragile and easily disruted.