Thermodynamic features of bile salt-human serum albumin interaction

Francesco Scagnolari; Aldo Roda; Adamo Fini; Brunella Grigolo

doi:10.1016/0167-4838(84)90019-0

Thermodynamic features of bile salt-human serum albumin interaction

Francesco Scagnolari, Aldo Roda, Adamo Fini, Brunella Grigolo

Istituti Ortopedici Rizzoli

Research output: Contribution to journal › Article › peer-review

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
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	https://doi.org/10.1016/0167-4838(84)90019-0
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

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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.",

keywords = "(Human serum), Albumin-bile salt interaction, Bile salt, Cholate, Hydrophobic interaction",

author = "Francesco Scagnolari and Aldo Roda and Adamo Fini and Brunella Grigolo",

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AU - Scagnolari, Francesco

AU - Roda, Aldo

AU - Fini, Adamo

AU - Grigolo, Brunella

PY - 1984/12/7

Y1 - 1984/12/7

N2 - 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.

AB - 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.

KW - (Human serum)

KW - Albumin-bile salt interaction

KW - Bile salt

KW - Cholate

KW - Hydrophobic interaction

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