title: Thermodynamic analysis of calcium binding to frog parvalbumin.
abstract: The enthalpy of calcium binding to frog parvalbumin (Rana temporaria isoenzyme IVb, pI 4.75) has been measured by microcalorimetry. The reaction is exothermic; the heat of the reaction in 100 mM KCl, 50mM Tris, pH 8.0 at 12 degrees C is -19 kJ (mol site)-1 and -33 kJ (mol site)-1 in the presence of 1 mM magnesium. The shape of the titration curve indicates that the properties of the two calcium binding sites are different. The thermodynamic parameters measured for frog parvalbumin are compared with those of related parvalbumins from carp and whiting.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D066298:In Vitro Techniques; D008274:Magnesium / Q000378:metabolism; D009124:Muscle Proteins / Q000378:metabolism*; D010320:Parvalbumins / Q000378:metabolism*; D011487:Protein Conformation; D011896:Rana temporaria; D013816:Thermodynamics
chemical_list: D009124:Muscle Proteins; D010320:Parvalbumins; D008274:Magnesium; D002118:Calcium