par Prieels, Jean-Paul 
;Schlusselberg, Jean
Référence BBA - Protein Structure, 491, 1, page (76-81)
Publication Publié, 1977-03
;Schlusselberg, Jean Référence BBA - Protein Structure, 491, 1, page (76-81)
Publication Publié, 1977-03
Article révisé par les pairs
| Résumé : | α-Lactalbumin from human milk shows an heterogeneous behaviour when subjected to ion exchange chromatography with DEAE-Sephadex. Two components have been separated, showing identical patterns in the following studies: amino acid compositions, fluorescence and circular dichroism spectra, transition temperature of denaturation, antigenicity, lactose synthase specifying activity and hydrodynamic properties. After rechromatography of either peak, these two components appeared to be in equilibrium. This equilibrium varies with the temperature and the pH of chromatography. Moreover, an increase of n-alcohol concentration in the eluting buffer also induces an increase of the second protein peak eluting at higher ionic strength. These two peaks seem to be the result of some conformational change induced upon the binding of the protein to the solid anionic matrix. © 1977. |
