Kinetics of cadmium and terbium dissociation from calmodulin and its tryptic fragments.
The kinetics of cadmium and terbium dissociation from bovine testis calmodulin and its tryptic fragments have been studied by stopped-flow fluorescence methods, using the calcium indicator Quin 2. Studies of the tryptic fragments TR1C and TR2C, comprising the N-terminal or C-terminal half of calmodulin, have clearly identified cadmium binding sites I and II as the low-affinity (rapidly dissociating) sites and sites III and IV as the high-affinity (slowly dissociating) sites. Thus the site preference of cadmium is the same as that of calcium. For terbium, however, sites I and II are the high-affinity sites and sites III and IV are the low-affinity sites. Thus, the site preference or terbium is not the same as that of calcium and cadmium. In contrast to previous studies with calcium, we observe two kinetic processes for dissociation from sites III and IV for experiments with both cadmium and terbium. Possible models for the binding of metal ions are discussed.
D001665:Binding Sites; D001667:Binding, Competitive; D002118:Calcium / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D010446:Peptide Fragments / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013725:Terbium / Q000378:metabolism*; D014357:Trypsin
D002147:Calmodulin; D010446:Peptide Fragments; D013725:Terbium; D014357:Trypsin; D002118:Calcium