XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

Posters
76.
THERMAL STABILITY OF CYTOCHROME C AND α-LACTALBUMIN
COMPLEXES
Diana Fedunová 1 , Zuzana Flachbartová 2 , Jaroslava Bágeľová 1 ,
Zuzana Gažová 1 and Marián Antalík 1,2
1
Department of Biophysics, Institute of Experimental Physics SAS, Kosice, Slovakia
2
Institute of Chemical Sciences, Faculty of Science, P. J. Safarik University,
Kosice, Slovakia
Effective activation of apoptosis is one of the important tools for tumor cell treatment.
Cytochrome c (cyt c) plays relevant role during early phase of apoptosis after release
from mitochondria in vivo. A new approach is oriented to the study of the ability of cyt
c to induce apoptosis by its transport from extracellular location. The active transport
of cyt c to the cells requires complexation with compounds supporting this process.
We have studied interactions of cyt c with α-lactalbumin (α-LA) in order to find optimal
conditions for their complexation necessary for using these complexes in induction of
programmed cell death. We have found that α-LA has only negligible effect on cyt c heme
pocket within wide pH interval. The complex formation is accompanied by turbidity increase
even at low protein concentrations. Thermal stability of the complex depends on
protein concentration ratio and absolute concentration value. The properties of studied
complexes depend strongly on ionic strength.
Acknowledgements: This work was supported within the projects Nos. 26220120021,
26220120001, 26220220005, 2622022033 in frame of SF EU, Centre of Excellence of SAS
Nanofluid and VEGA 0056, 0038 and 0079.
XXII. Biochemistry Congress, Martin
199