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Polyclonal anti-idazoxan antibodies: characterization and purification
B Fatima1, G Hugues, B Giampiero
1Laboratoire de Pharmacologie Cardiovasculaire et Rénale, CNRS URA, Faculté de Médecine, Strasbourg, France.
Amino-idazoxan coupled to hemocyanine was used to raise anti-idazoxan antibodies in the rabbit. The antibodies were affinity purified with an amino-idazoxan affinity column. Binding studies with [3H]idazoxan showed a dissociation constant of 2.2 +/- 1.4 nM. The specificity spectrum of these antibodies indicates that the imidazoline part of idazoxan is more important for recognition than the benzodioxan ring as imidazoline substances (clonidine, cirazoline) are powerful competitors of [3H]idazoxan binding on the antibodies. Catecholamines or imidazoles were unable to displace [3H]idazoxan from the antibodies. These anti-idazoxan antibodies present specificity similarities with the imidazoline receptor as did our previously obtained anti-clonidine antibodies. Affinity-purified antibodies represent useful tools for studying the imidazoline receptors particularly with an anti-idiotypic approach.
Amino-idazoxan coupled to hemocyanine was used to raise anti-idazoxan antibodies in the rabbit. The antibodies were affinity purified with an amino-idazoxan affinity column. Binding studies with [3H]idazoxan showed a dissociation constant of 2.2 +/- 1.4 nM. The specificity spectrum of these antibodies indicates that the imidazoline part of idazoxan is more important for recognition than the benzodioxan ring as imidazoline substances (clonidine, cirazoline) are powerful competitors of [3H]idazoxan binding on the antibodies. Catecholamines or imidazoles were unable to displace [3H]idazoxan from the antibodies. These anti-idazoxan antibodies present specificity similarities with the imidazoline receptor as did our previously obtained anti-clonidine antibodies. Affinity-purified antibodies represent useful tools for studying the imidazoline receptors particularly with an anti-idiotypic approach.