Thermodynamic data on the binding of six M2(+)-ions to bovine, goat, and human alpha-lactalbumin.
By batch microcalorimetry we titrated the apo-forms of bovine, goat, and human alpha-lactalbumin with Mg2+, Ca2+, Sr2+, Ba2+, Mn2+, and Cd2+ ions at pH 7.5 and 25 degrees C. The titration curves enabled us to calculate the apparent enthalpy changes and binding constants and thus, also the free energy and the entropy changes of the binding. CD-spectra showed that all cations induce the same conformational change to the native form of the protein. The calorimetric and spectroscopic results, as well as sequence comparisons confirm the hypothesis that all these ions occupy the very same site on the molecule. The thermodynamic parameters, plotted vs the ionic radii, run parallel for the three proteins, which illustrates the earlier proposed "rigid site" model.
Desmet
J
J
Interdisciplinair Research Center, K. U. Leuven Campus Kortrijk, Belgium.
Haezebrouck
P
P
Van Cauwelaert
F
F
D000818:Animals; D001665:Binding Sites; D002151:Calorimetry; D002413:Cations, Divalent; D002417:Cattle; D006041:Goats; D006801:Humans; D007700:Kinetics; D007768:Lactalbumin / Q000737:chemistry / Q000378:metabolism*; D008670:Metals / Q000378:metabolism*; D013816:Thermodynamics
D002413:Cations, Divalent; D008670:Metals; D007768:Lactalbumin