Thermal aggregation of bovine serum albumin at different pH: comparison with human serum albumin |
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Authors: | Valeria Vetri Fabio Librizzi Maurizio Leone Valeria Militello |
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Institution: | (1) Dipartimento di Scienze Fisiche ed Astronomiche, Università di Palermo, Via Archirafi 36, 90123 Palermo, Italy;(2) Consiglio Nazionale delle Ricerche, Istituto di Biofisica, Unità di Palermo, Palermo, Italy |
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Abstract: | We report here a study on thermal aggregation of BSA at two different pH values selected to be close to the isoelectric point
(pI) of this protein. Our aim is to better understand the several steps and mechanisms accompanying the aggregation process.
For this purpose we have performed kinetics of integrated intensity emission of intrinsic and extrinsic dyes, tryptophans
and ANS respectively, kinetics of Rayleigh scattering and of turbidity. The results confirm the important role played by conformational
changes in the tertiary structure, especially in the exposure of internal hydrophobic regions that promote intermolecular
interactions. We also confirm that the absence of electrostatic repulsion favours the disordered non-specific interactions
between molecules and consequently affects the aggregation rate. Finally, the comparison between BSA and another relative
protein, HSA, allows us to clarify the role of different domains involved in the aggregation process.
Proceedings of the XVIII Congress of the Italian Society of Pure and Applied Biophysics (SIBPA), Palermo, Sicily, September
2006. |
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