Purification and some physicochemical properties of bovine kappa-casein.

Autor: Vreeman HJ, Both P, Brinkhuis JA, van der Spek C
Jazyk: angličtina
Zdroj: Biochimica et biophysica acta [Biochim Biophys Acta] 1977 Mar 28; Vol. 491 (1), pp. 93-103.
DOI: 10.1016/0005-2795(77)90044-7
Abstrakt: 1. A description is given of the fractionation of kappa-casein on DEAE-cellulose using a pH gradient. With this method an improved separation of the kappa-casein components with a higher negative charge is obtained. 2. It is shown that at least one of the kappa-casein fractions has a second phosphate ester group. The heterogeneity of kappa-casein therefore is not exclusively caused by a varying N-acetylneuraminic acid content. 3. Ultracentrifuge experiments and exclusion gel chromatography show that the purified kappa-casein fraction having the lowest electrophoretic mobility exhibits a monomer-polymer association equilibrium. The free energy of association per mol monomer in 0.2 M NaCl is approximately --36 kJ-mol-1.
Databáze: MEDLINE