Lead ion effect on creatine kinase: equilibrium and kinetic studies of inactivation and conformational changes

The International Journal of Biochemistry & Cell Biology
Hong-Wei ZhouHai-Meng Zhou

Abstract

The effects of lead ions on creatine kinase (CK) were studied by measuring activity changes, intrinsic fluorescence spectra and 8-anilo-1-naphthalenesulfonate (ANS)-binding fluorescence along with size-exclusion chromatography (SEC). Below 5 mM Pb(2+) concentration, there was nearly no change of the enzyme activity and a slight change of the ANS-binding fluorescence. The CK activity decreased significantly from 10 to 25 mM Pb(2+) concentrations. No residual activity was observed above 25 mM Pb(2+). The kinetic time courses of inactivity and unfolding were all mono-phase courses with the inactivation rate constants being greater than the unfolding rate constants for the same Pb(2+) concentration. The changes in fluorescence maximum and fluorescence intensity were relatively slow for 40-80 mM Pb(2+) as well as in the initial stage for less than 5 mM Pb(2+), showing that two transition states exist for Pb(2+) induced equilibrium-unfolding curves. The intrinsic fluorescence spectra and ANS-binding fluorescence measurements showed that even for high Pb(2+) concentrations, CK did not fully unfold. Additionally, the SEC results showed that the enzyme molecule still existed in an inactive dimeric state at 20 and 40 mM Pb(2+) solutions....Continue Reading

References

Jan 1, 1985·Annual Review of Biochemistry·S P Bessman, C L Carpenter
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Citations

Mar 31, 2004·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·G GiannacciniA Lucacchini

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