Differential scanning calorimetry of lobster haemocyanin.
Differential scanning calorimetry has been performed with Palinurus vulgaris haemocyanin monomers and hexamers. The denaturation of the protein is irreversible. Both the temperature of the transition maximum and the enthalpy are lower for the monomer than for the hexamer. A scan rate dependence of the temperature of the maxima is found for both the monomer and the hexamer; for the hexamer at least, this can be explained in terms of a two-state kinetic model. Some comments are made as to the use of equilibrium thermodynamics in the analysis of irreversible scanning calorimetric traces.
Guzmán-Casado
M
M
Departamento de Química-Fisica, Facultad de Ciencias, Universidad de Granada, Spain.
Parody-Morreale
A
A
Mateo
P L
PL
Sánchez-Ruiz
J M
JM
D000818:Animals; D002152:Calorimetry, Differential Scanning; D006433:Hemocyanins / Q000032:analysis; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008433:Mathematics; D008121:Nephropidae; D011489:Protein Denaturation; D013816:Thermodynamics
D006433:Hemocyanins