The fatty-acid-induced conformational states of human serum albumin investigated by means of multiple co-binding of protons and oleic acid

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 unde...

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Bibliographic Details
Published in:Biochemical journal 1988-03, Vol.250 (2), p.443-446
Main Authors: Dröge, J H, Janssen, L H, Wilting, J
Format: Article
Language:English
Subjects:
albumin
Binding Sites
Circular Dichroism
Diazepam - metabolism
Humans
Hydrogen-Ion Concentration
Ligands
man
Oleic Acid
Oleic Acids - pharmacology
Oxyphenbutazone - metabolism
Protein Conformation - drug effects
Protons
Serum Albumin - metabolism
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Summary: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.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2500443