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Thermodynamics of water binding by human serum albumin suspended in acetonitrile

✍ Scribed by Mikhail D. Borisover; Vladimir A. Sirotkin; Boris N. Solomonov

Publisher
Elsevier Science
Year
1995
Tongue
English
Weight
326 KB
Volume
254
Category
Article
ISSN
0040-6031

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Binding sites on human serum albumin (HSA) for anionic drugs and fatty acids have been thermodynamically characterized by microcalorimetry. The binding and the thermodynamic parameters were directly computed from the calorimetric titration data at 37 "C in a phosphate buffer (pH 7.4) using one-and t