These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: The fatty-acid-induced conformational states of human serum albumin investigated by means of multiple co-binding of protons and oleic acid.
    Author: Dröge JH, Janssen LH, Wilting J.
    Journal: Biochem J; 1988 Mar 01; 250(2):443-6. PubMed ID: 2833243.
    Abstract:
    The binding of oleic acid to human serum albumin causes progressive changes in (a) the pK of some amino acid residues, as detected by pH-stat titration and (b) the induced molar ellipticities of albumin-bound drugs (diazepam and oxyphenbutazone), as measured by c.d. It is concluded that albumin undergoes several conformational transitions as the amount of oleic acid bound increases from 0 to about 9 molecules/molecule of protein. At least three different conformations of the protein seem to be involved. These conformations can be linked with the three classes of oleic acid-binding sites on albumin.
    [Abstract] [Full Text] [Related] [New Search]