Structural differences between bovine A1 and A2 β-casein alter micelle self-assembly and influence molecular chaperone activity
نویسندگان
چکیده
منابع مشابه
Self-assembly of β-casein and lysozyme
The self-assembly of β-casein and lysozyme, a linear and a globular protein with isoelectric point of pH 5.0 and 10.7, respectively, was studied. Polydisperse electrostatic complex micelles formed when mixing β-casein and lysozyme aqueous solutions. After the micelle solution was heated, lysozyme gelated and β-casein was trapped in the gel, producing narrowly dispersed nanoparticles. The nanopa...
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متن کاملThe chaperone ability comparison of norma II-casein and modified d-casein upon interaction with lysozinie
Diminishing protein aggregation by chaperone is very important factor in medicine and industry. In this paper, itis induced the chaperone ability for 0-casein upon modification of its acidic residues by Woodward reagentK(WRK) and examined on lysozyme as a target protein at pH 7.2 and outlined the mechanism for chaperoneability of modified system by UV-Vis and fluorescence spectroscopy and theor...
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ژورنال
عنوان ژورنال: Journal of Dairy Science
سال: 2015
ISSN: 0022-0302
DOI: 10.3168/jds.2014-8800