5-(dimethylamino)naphthalene-1-sulfonic acid, a fluorescent probe of the medium chain fatty acid binding site of serum albumin. Academic Article uri icon

Overview

abstract

  • Reversible binding of 5-(dimethylamino)-naphthalene-1-sulfonic acid (DNS) to human and bovine serum albumin has been monitored by changes in fluorescence intensity, wavelength maxima, and polarization. DNS has only one major binding site (ka = 5 x 10(6)) and one minor site (ka = 3 x 10(5)) on these proteins. The probe is competitively displaced from its high-affinity site by medium chain fatty acids and by N-acetyl-L-tryptophan. The binding site for DNS is highly hydrophobic and is considerably less polar than the hydrocarbon region of lipid bilayers. Resonance energy transfer indicates that the binding site is located 20.7 +/- 2 A from the single tryptophan residue of human serum albumin.

publication date

  • January 5, 1982

Research

keywords

  • Dansyl Compounds
  • Fatty Acids
  • Serum Albumin

Identity

Scopus Document Identifier

  • 0020475134

PubMed ID

  • 7059578

Additional Document Info

volume

  • 21

issue

  • 1