Thermodynamics of water binding by human serum albumin suspended in acetonitrile

Heat effects resulting from the introduction of solid human serum albumin (HSA) into various water-acetonitrile mixtures were measured calorimetrically at 298 K. The amount of water bound to the suspended HSA as a function of the water content of the solvent was also determined. Introducing HSA into...

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Bibliographic Details
Published in:Thermochimica acta 1995-04, Vol.254, p.47-53
Main Authors: Borisover, Mikhail D., Sirotkin, Vladimir A., Solomonov, Boris N.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Chemistry
Exact sciences and technology
Fundamental and applied biological sciences. Psychology
Gas-liquid interface and liquid-liquid interface
General and physical chemistry
Holoproteins
HSA
Human serum albumin
Organic solvent
Other proteins
Proteins
Surface physical chemistry
Thermodynamics
Water sorption
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Summary:Heat effects resulting from the introduction of solid human serum albumin (HSA) into various water-acetonitrile mixtures were measured calorimetrically at 298 K. The amount of water bound to the suspended HSA as a function of the water content of the solvent was also determined. Introducing HSA into water-acetonitrile mixtures involves water binding according to the Langmuir isotherm with an adsorption constant K c = 1.0 ± 0.1 M −1, enthalpy Δh = −9.0 ± 1.5 kJ mol −1 and entropy ΔS = −30 ± 6 J mol −1 K −1. Placing HSA in the solvent has an additional heat effect of 46 ± 19 J g −1, which is attributed to an unknown transformation of the protein preparation.
ISSN:0040-6031
1872-762X
DOI:10.1016/0040-6031(94)02108-Z