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Human serum albumin unfolding pathway upon drug binding: A thermodynamic and spectroscopic description

✍ Scribed by Mohammad Arif Cheema; Pablo Taboada; Silvia Barbosa; Josué Juárez; Manuel Gutiérrez-Pichel; Mohammad Siddiq; Víctor Mosquera


Book ID
118475157
Publisher
Elsevier Science
Year
2009
Tongue
English
Weight
436 KB
Volume
41
Category
Article
ISSN
0021-9614

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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