Ak. Bordbar et al., COMPARATIVE THERMODYNAMIC STABILITY OF BOVINE AND PIGEON HEMOGLOBINS BY INTERACTION WITH SODIUM N-DODECYL SULFATE, Thermochimica acta, 287(2), 1996, pp. 343-349
The binding of sodium n-dodecyl sulphate (SDS) to pigeon and bovine ha
emoglobin has been studied at pH 6.4 and 25 degrees C by equilibrium d
ialysis and titration microcalorimetry techniques. The thermodynamic p
arameters of these interactions have been determined by application of
the Wyman binding potential concept and interpreted from a structural
viewpoint. A comparison of the results shows that bovine haemoglobin
has more thermodynamic stability than pigeon haemoglobin. From this, a
reason for the high oxygen affinity of avian haemoglobin is proposed.