RT Journal Article
SR Electronic
T1 Immunochemical Characterization of a Lysergyl Derivative Incorporated into Protein
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP 767
OP 775
VO 10
IS 5
A1 DENNIS E. LOPATIN
A1 JEFFREY L. WINKELHAKE
A1 EDWARD W. VOSS, JR.
YR 1974
UL http://molpharm.aspetjournals.org/content/10/5/767.abstract
AB A derivative of d-lysergic acid diethylamide (LSD), lysergylder, previously shown to be covalently coupled to secreted low molecular weight peptides, was shown during incubation in vitro of immune lymphoid cells with LSD to possess structural features closely resembling the parent molecule. Binding studies of LSD and lysergylder ligands with antibodies directed against both lysergic acid and lysergylder suggested that both antibodies possessed similar specificity. [3H]LSD and [3H]lysergylder were bound by anti-lysergyl antibody with average intrinsic association constants (K0) of 3.5 x 105 M-1 and 7.8 x 105 M-1, respectively. Both ligands were bound by anti-lysergylder antibody with K0 values of 1-2 x 105 M-1. Single-point equilibrium dialysis experiments indicated that both antibody populations bound the derivative in preference to LSD. Mild alkaline hydrolysis of LSD was shown to generate a molecular species which was bound by anti-1ysergylder antibody with the same energy as lysergylder. Alkaline hydrolysis had no effect on lysergylder. These data suggest generation of a demethylated derivative of LSD during incubation of LSD in vitro.