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Advances in Physical Chemistry
Volume 2013 (2013), Article ID 360239, 8 pages
Research Article

Study of Bovine Serum Albumin Solubility in Aqueous Solutions by Intrinsic Viscosity Measurements

Instituto de Física Aplicada-CONICET, Facultad de Química, Bioquímica y Farmacia, Universidad Nacional de San Luis, Área de Química Física, Chacabuco 917, 5700 San Luis, Argentina

Received 25 March 2013; Accepted 9 May 2013

Academic Editor: Sylvio Canuto

Copyright © 2013 Martin Alberto Masuelli. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The behavior of bovine serum albumin (BSA) in water is scarcely studied, and the thermodynamic properties arising from the experimental measurements have not been reported. Intrinsic viscosity measurements are very useful in assessing the interaction between the solute and solvent. This work discussed in a simple determination of the enthalpy of BSA in aqueous solution when the concentration ranges from 0.2 to 36.71% wt. and the temperature from 35 to C. The relationship between the concentration and intrinsic viscosity is determined according to the method of Huggins. The temperature increase reduces the ratio between inherent viscosity and concentration (). This is reflected in the Van't Hoff curve. Furthermore, this work proposes hydrodynamic cohesion value as an indicator of the degree of affinity of protein with water and thermodynamic implications in conformational changes.