The binding of Cu 2+  to actin without loss of polymerizability: the involvement of the rapidly reacting -SH group.
D000199:Actins; D002118:Calcium; D002127:Calcium Isotopes; D055598:Chemical Phenomena; D002621:Chemistry; D002729:Chloromercuribenzoates; D002942:Circular Dichroism; D003300:Copper; D004492:Edetic Acid; D004578:Electron Spin Resonance Spectroscopy; D005033:Ethylmaleimide; D006639:Histidine; D007700:Kinetics; D046911:Macromolecular Substances; D009124:Muscle Proteins; D011485:Protein Binding; D011489:Protein Denaturation; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D013438:Sulfhydryl Compounds; D014364:Tryptophan; D014466:Ultraviolet Rays
D000199:Actins; D002127:Calcium Isotopes; D002729:Chloromercuribenzoates; D046911:Macromolecular Substances; D009124:Muscle Proteins; D013438:Sulfhydryl Compounds; D006639:Histidine; D003300:Copper; D014364:Tryptophan; D004492:Edetic Acid; D005033:Ethylmaleimide; D002118:Calcium