The chaperone ability comparison of norma II-casein and modified d-casein upon interaction with lysozinie

Subject Areas : Journal of Physical & Theoretical Chemistry

H. Rajabzadeh ¹ , D. Nourouzian ² , K. Zare ³ , F. Mollaamin ⁴

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Received: 2015-05-30 Accepted : 2015-05-30 Published : 2010-05-01

Keywords: Modified ffeasein, Lysoiyme: Hydrophobicity, Disaggregatiorr, Woodward's re,

Abstract :

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 theoretical calculation methods.

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The chaperone ability comparison of norma II-casein and modified d-casein upon interaction with lysozinie