Comparative
study of thermal stability of healthy and focal segmental glomerulosclerosis
plasma albumin |
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Authors: | M Bruschi L Musante G M Ghiggeri G Rialdi G Candiano |
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Institution: | (1) RenalChild Foundation, Genoa, Italy;(2) Laboratory on Pathophysiology of Uremia, G. Gaslini Children Hospital, Genoa, Italy |
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Abstract: | The thermodynamic parameters calculated from measurements obtained by
differential scanning calorimetry from healthy and focal segmental glomerulosclerosis
albumin are reported. The same values were determined by fluorescence spectra
and by the second derivative absorption spectra and they resulted in agreement
with values obtained from the calorimetry technique. Nevertheless the unfolding
mechanism seems to be completely altered when pathological albumin is compared
with healthy albumin. The C
p
values measured by calorimetry show an increase with mild slope with healthy
protein; on the contrary the slope intensely increase with pathological protein.
Furthermore the λmax of this molecule is lower
and drastically decrease with the increase of temperature when compared with
healthy one.
Therefore the modification of cys 34 on pathological
albumin is supposed to cause an alteration of the structure, the swelling
and the unfolding mechanism. |
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Keywords: | albumin differential scanning calorimetry (DSC) focal segmental glomerulosclerosis (FSGS) intrinsic fluorescence plasma second derivative UV spectrum |
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