Ukr.Biochem.J. 2011; Volume 83, Issue 3, May-Jun, pp. 65-75

Peculiarities of secondary structure of serum albumin of some representatives of the animal kingdom

G. V. Pekhimenko1, T. M. Kuchmerovska2

1Vernadsky Taurian National University, Simferopol, Ukraine;
2Palladin Institute of Biochemistry National Academy of Science of Ukraine, Kyiv;

Methods of infrared (IR) spectroscopy and circular dichroism (CD) are suitable techniques for detection of proteins structural changes. These methods were used for determinating peculiarities of the secondary structure of serum albumins in some representatives of two classes of reptiles: Horsfield’s tortoise (Testudo horsfieldi), water snake (Natrix tessellata) and grass snake (Natrix natrix) and birds: domestic goose (Anser anser), domestic chicken (Gallus domesticus), domestic duck (Anas platyrhyncha) and dove colored (Columba livia). An analysis of IR spectra and spectra obtained by the method of CD of serum albumins of both classes representatives revealed that β-folding structure and α-helical sections that form the α-conformation play an important role in conformational structure formation of polypeptide chain and also disordered sites of molecules of these proteins. It was observed that certain redistribution depending on animals species exists, in the formation of secondary structure of serum albumins of the investigated representatives of reptiles and birds classes between the content of β-folding structure, α-helical sections and disordered sites in molecules of these proteins.

Keywords: , , , ,

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