Abstract
Interaction with human serum albumin is responsible for important aspects of the physiological behaviour of bile salts, although this factor has not been adequately examined. The nature of the binding is investigated here by means of thermodynamic parameters determined by equilibrium dialysis and microcalorimetric measurements. The positive enthalpy and entropy values obtained indicate the presence of a poorly specific hydrophobic bonding.
Original language | English |
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Pages (from-to) | 274-277 |
Number of pages | 4 |
Journal | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
Volume | 791 |
Issue number | 2 |
DOIs | |
Publication status | Published - Dec 7 1984 |
Keywords
- (Human serum)
- Albumin-bile salt interaction
- Bile salt
- Cholate
- Hydrophobic interaction
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
- Structural Biology