Journal of Paramedical Sciences. 2011; 2 (1): 13-19
in English
| IMEMR
| ID: emr-194723
ABSTRACT
Molecular chaperones are characterized by a general behavior, arresting the exposed hydrophobic surfaces of denaturing substrate proteins. In the present study, the capacity of beta -caseins [beta -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 beta -CNs [camel, bovine]. Bovine beta -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
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Index:
IMEMR (Eastern Mediterranean)
Language:
English
Journal:
J. Paramed. Sci.
Year:
2011
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