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

الموضوعات : Journal of Physical & Theoretical Chemistry

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

1 - -
2 - -
3 - -
4 - -

تاريخ الإرسال : 12 السبت , شعبان, 1436 تاريخ التأكيد : 12 السبت , شعبان, 1436 تاريخ الإصدار : 17 السبت , جمادى الأولى, 1431

الکلمات المفتاحية: Modified ffeasein, Lysoiyme: Hydrophobicity, Disaggregatiorr, Woodward's re,

ملخص المقالة :

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.