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  • Title: Binding of a dihydropyridine felodipine-analogue to calmodulin and related calcium-binding proteins.
    Author: Boström SL, Westerlund C, Rochester S, Vogel HJ.
    Journal: Biochem Pharmacol; 1988 Oct 01; 37(19):3723-8. PubMed ID: 3178884.
    Abstract:
    A dihydropyridine-affinity column was prepared by coupling a physiologically active and vasoselective amino-derivative of felodipine to divinylsulfone-activated Trisacryl GF2000. Calmodulin (CaM) as well as the homologous calcium-binding proteins skeletal and cardiac Troponin C (sTnC and cTnC) and S100b bound to this resin in a calcium-dependent manner. In contrast, other homologous proteins such as parvalbumin and the intestinal calcium-binding protein did not bind. Competition studies showed that CaM had a higher affinity for the felodipine-column than sTnC or cTnC. Through studies with a series of proteolytic fragments of CaM and sTnC, it was found that the felodipine binding site is located in the amino-terminal domain of the protein. These results illustrate the utility of affinity-chromatography for the study of dihydropyridine-binding proteins.
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