Dephosphorylation of αs- and β -Caseins and Its Effect on Chaperone Activity: A Structural and Functional Investigation
Date
2009
Authors
Koudelka, Tomas
Hoffmann, Peter
Carver, John
Journal Title
Journal ISSN
Volume Title
Publisher
American Chemical Society
Abstract
Milk casein proteins can act as molecular chaperones: under conditions of stress, such as elevated temperature, molecular chaperones stabilize proteins from unfolding, aggregating, and precipitating. In this study, αS- and β-caseins were dephosphorylate
Description
Keywords
Keywords: alkaline phosphatase; casein; chaperone; article; chemistry; circular dichroism; metabolism; phosphorylation; physiology; protein folding; spectrofluorometry; static electricity; structure activity relation; Alkaline Phosphatase; Caseins; Circular Dichroi Amyloid fibril; Casein proteins; Molecular chaperone; Protein aggregation
Citation
Collections
Source
Journal of Agricultural and Food Chemistry
Type
Journal article
Book Title
Entity type
Access Statement
License Rights
Restricted until
2037-12-31