Studies on the molecular chaperone abilities of alphaS1- and alphaS2-casein from bovine milk

Authors

Teresa M. Treweek, University of WollongongFollow
William E. Price, University of WollongongFollow
John A. Carver, University of AdelaideFollow

RIS ID

61431

Publication Details

T. M. Treweek, W. E. Price & J. A. Carver (2006). Studies on the molecular chaperone abilities of alphaS1- and alphaS2-casein from bovine milk. Riddet Centre, Massey University, Palmerston North, New Zealand., 16th February 2006.

Abstract

α_s-Casein is a predominant milk protein with important nutritional properties. In addition it has been shown to have molecular chaperone properties similar to those of the sHsps (small heat-shock proteins) and cIusterin. In order to study their relative contributions to the chaperone ability of total α_s-casein, the individual subunits, α_s1- and α_s2-casein, which are present in a ratio of approximately 4:1 (α_s1:α_s2) in bovine milk were separated and purified from commercially obtained α_s-casein. Anion-exchange chromatography was performed in a denaturing and reducing imidazole-Hel buffer at pH 7 as per Thompson et al. (1966) with minor changes, dialyzed against a urea gradient and lyophilized in ammonium acetate buffer.