5-(Dimethylamino)naphthalene-1 -sulfonic Acid, a Fluorescent Probe of the Medium Chain Fatty Acid Binding Site of Serum Albumin

Michael C. Doody, Antonio M. Gotto, Louis C. Smith

Research output: Contribution to journalArticle

7 Scopus citations

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 × 106) and one minor site (ka = 3 × 105) 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 Å from the single tryptophan residue of human serum albumin.

Original languageEnglish (US)
Pages (from-to)28-33
Number of pages6
JournalBiochemistry
Volume21
Issue number1
DOIs
StatePublished - Jan 1982

ASJC Scopus subject areas

  • Biochemistry

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