%0 Journal Article
%T A Comparative study on the chaperone-like activity of camel and bovine ¦Â-caseins
%A Mehran Miroliaei
%A Mozhgan Shirazi
%A Reza Yousefi
%J Journal of Paramedical Sciences
%D 2011
%I Shahid Beheshti University of Medical Sciences
%X Molecular chaperones are characterized by a general behavior, arresting the exposed hydrophobic surfaces of denaturing substrate proteins. In the present study, the capacity of ¦Â-caseins (¦Â-CN) from camel and bovine milk in suppression of thermal aggregation process of apo-yeast alcohol dehydrogenase (YADH) was assessed. Apo-I enzyme was prepared by removal of the structural zinc; while apo-II-protein was obtained by depleting conformational and catalytic zinc atoms. Fluorescence spectroscopy using ANS probe revealed greater hydrophobic surface in apo-II ADH. Considerable decrease in aggregation of the heat treated protein molecules was observed upon exposing to ¦Â-CNs (camel, bovine). Bovine ¦Â-CN afforded more adverse effects on thermal aggregation. A direct correlation between casein¡¯s chaperone activity and structural stability of the substrate proteins was displayed. Moreover, an association between casein source and chaperone-like activity is suggested.
%K ¦Â-casein
%K Aggregation
%K Yeast Alcohol Dehydrogenase
%K Apo-Enzyme
%K Aggregation
%K 8 Anilino-1-Naphthalenesulfonic Acid (ANS).
%U http://journals.sbmu.ac.ir/jps/article/view/2142/1831