ISSN:
1432-1017
Keywords:
α-lactalbumin
;
Metal ion binding
;
Thermodynamics
;
Microcalorimetry
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Physics
Notes:
Abstract By means of reaction calorimetry we measured the apparent enthalpy change, ΔHapp, of the binding of Mn2+-ions to goat α-lactalbumin as a function of temperature. The observed ΔHapp can be written as the sum of contributions resulting from a conformational and a binding process. In combination with the thermal unfolding curve of goat α-lactalbumin, we succeeded in separating the complete set of thermodynamic parameters (ΔH, ΔG, ΔS, ΔCp) into the binding and conformational contributions. By circular dichroism we showed that NH 4 + -ions, upon binding to bovine a-lactalbumin, induce the same conformational change as do Na+ and K+: the binding constant $$K_{NH_4^ + }^{app} $$ equals 98 ± 9 M−1.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00450561
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