Abstract
As a result of the recent disclosure of the striking similarities between the covalent structures of bovine α-lactalbumin and of hen egg-white lysozyme, comparative physicochemical properties of α-lactalbumins and lysozymes of various sources seemed worth investigating. Therefore human milk α-lactalbumin and human milk or urinary lysozyme were purified. Their physical properties were examined in order to study the extent of similarity of the three-dimensional structure when considering the two proteins from the same species. Diffusion and sedimentation experiments showed that the hydrodynamic shape and the molecular weight of human α-lactalbumin and lysozyme were strikingly comparable. Concerning the secondary structure, it was observed by optical rotatory dispersion and circular dichroism that human lysozyme displays slightly more helix than human α-lactalbumin. Furthermore, when considering thermal denaturation, the transition temperatures and changes in enthalpy or entropy are all markedly lower for human α-lactalbumin than for lysozyme. These findings have been discussed in relation to the physicochemical properties of bovine α-lactalbumin and egg-white lysozyme.
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