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Thermodynamic analysis of calcium binding to frog parvalbumin

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Summary

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 100mm KCl, 50mm Tris, pH 8.0 at 12° C is −19 kJ (mol site)−1 and −33 kJ (mol site)−1 in the presence of 1mm 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.

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  1. S. J. Smith

    Present address: Department of Biochemistry, University of Arizona, Biological Sciences West, 85721, Tucson, Arizona, USA

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  1. Department of Physiology, University College London, Gower Street, WC1E 6BT, London

    S. J. Smith & R. C. Woledge

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Smith, S.J., Woledge, R.C. Thermodynamic analysis of calcium binding to frog parvalbumin. J Muscle Res Cell Motil 6, 757–768 (1985). https://doi.org/10.1007/BF00712240

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