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

محورهای موضوعی : Journal of Physical & Theoretical Chemistry

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

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تاریخ دریافت : 1394/03/09 تاریخ پذیرش : 1394/03/09 تاریخ انتشار : 1389/02/11

کلید واژه: Modified ffeasein, Lysoiyme: Hydrophobicity, Disaggregatiorr, Woodward's re,

چکیده مقاله :

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.