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Protein dilution effect on thiouracil-seroalbumin interactions.

Authors
  • Ochoa de Aspuru, E
  • Marquínez, M A
  • Zatón, A M
Type
Published Article
Journal
Biophysical Chemistry
Publisher
Elsevier
Publication Date
Dec 01, 1997
Volume
69
Issue
2-3
Pages
233–237
Identifiers
PMID: 9474756
Source
Medline
License
Unknown

Abstract

As the spectra and binding parameters calculated for the thiouracil-albumin interaction change with the protein concentration, a human seroalbumin conformational change depending on protein concentration has been suggested. This protein-conformational change is tested by dilatometry and viscosimetry. At low concentrations, albumin showed a greater thiouracil binding capacity and a second positive peak in its interaction with the drug, detected by difference spectroscopy. Both effects are due to a monomerisation of protein dimers and not to a conformational change depending on protein concentration. This monomerisation would imply a major accessibility of thiouracil and propylthiouracil to other binding sites on HSA.

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