TY - JOUR
T1 - A native 13-kDa fatty acid binding protein from the liver fluke Fasciola hepatica
AU - Deevska, G.
AU - Timanova-Atanasova, A.
AU - Jordanova, R.
AU - Barrett, John
AU - Bankov, I.
AU - Radoslavov, G.
N1 - Timanova-Atanasova, A., Jordanova, R., Radoslavov, G., Deevska, G., Bankov, I., Barrett, J. (2004). A native 13-kDa fatty acid binding protein from the liver fluke Fasciola hepatica. Biochimica et Biophysica Acta-General Subjects, 1674, (2), 200-204.
Sponsorship: Deutsche Forshungsgemeinschaft (DFG)
PY - 2004/9/24
Y1 - 2004/9/24
N2 - A 13-kDa fatty acid binding protein (FABP) (Fh13) has been isolated from the cytosol of adult Fasciola hepatica and its physicochemical and binding characteristics determined. Fh13 appears to exist as a dimer in native solution. Binding of the fluorescent fatty acid analogue 11-((5-dimethyl aminonaphthalene-1-sulfonyl) amino) undecanoic acid (DAUDA) to Fh13 results in changes in the emission spectrum, which are reversed by oleic acid. The binding activity for DAUDA determined from titration experiments revealed a single binding site per monomeric unit with Kd of 1.5 μM. The displacement of DAUDA by competitive nonfluorescent ligands allowed Kd values for oleic (2.5 μM), retinoic (2.8 μM), palmitic (4.1 μM) and arachidonic acid (6.1 μM) to be calculated. Ten commonly used anthelmintics were evaluated for binding to Fh13, but only bithionol showed binding activity commensurate with those of the putative natural ligands (Kd 6.8 μM).
AB - A 13-kDa fatty acid binding protein (FABP) (Fh13) has been isolated from the cytosol of adult Fasciola hepatica and its physicochemical and binding characteristics determined. Fh13 appears to exist as a dimer in native solution. Binding of the fluorescent fatty acid analogue 11-((5-dimethyl aminonaphthalene-1-sulfonyl) amino) undecanoic acid (DAUDA) to Fh13 results in changes in the emission spectrum, which are reversed by oleic acid. The binding activity for DAUDA determined from titration experiments revealed a single binding site per monomeric unit with Kd of 1.5 μM. The displacement of DAUDA by competitive nonfluorescent ligands allowed Kd values for oleic (2.5 μM), retinoic (2.8 μM), palmitic (4.1 μM) and arachidonic acid (6.1 μM) to be calculated. Ten commonly used anthelmintics were evaluated for binding to Fh13, but only bithionol showed binding activity commensurate with those of the putative natural ligands (Kd 6.8 μM).
U2 - 10.1016/j.bbagen.2004.06.018
DO - 10.1016/j.bbagen.2004.06.018
M3 - Article
SN - 1872-8006
VL - 1674
SP - 200
EP - 204
JO - Biochimica et Biophysica Acta (BBA) - General Subjects
JF - Biochimica et Biophysica Acta (BBA) - General Subjects
IS - 2
ER -