αs-casein inhibits the pressure-induced aggregation of β-lactoglobulin through its molecular chaperone-like properties

Author:

He Jin-Song,Zhu Songming,Mu Tai-Hua,Yu Yong,Li Jianping,Azuma Norihiro

Publisher

Elsevier BV

Subject

General Chemical Engineering,General Chemistry,Food Science

Reference34 articles.

1. Molecular chaperone-like properties of an unfolded protein, αs-casein;Bhattacharyya;Journal of Biological Chemistry,1999

2. Pressure denaturation of β-lactoglobulin;Botelho;European Journal of Biochemistry,2000

3. Interactions of milk proteins during heat and high hydrostatic pressure treatments – a review;Considine;Innovative Food Science & Emerging Technologies,2007

4. Secondary structure of bovine αS1- and β-casein in solution;Creamer;Archives of Biochemistry and Biophysics,1981

5. On the substrate specificity of α-crystallin as a molecular chaperone;Das;Biochemical Journal,1995

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