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Lopatin DE, Voss EW. 
“Anti-Lysergic Antibody: Measurement of Binding Parameters in IgG Fractions.”. 
Immunochemistry. 1974;11(6):285-293.
Binding parameters in IgG fractions of anti-lysergyl antisera were measured. Methods Antisera were prepared by injecting rabbits in the hind foot pads and intrascapularly with a total of 5 mg lysergyl poly-L-lysine complexed to succinylated keyhole limpet hemocyanin in Freund's adjuvant. Antibody binding affinity was measured by equilibrium dialysis. Immunoadsorption was carried out using DNP-BSA-bromoacetylcellulose. Results Results of the dialysis binding assay were similar to those obtained in a radioimmuneassay, but the background in the radio-immunoassay was 2 times greater. (3) - Lysergic acid diethyl-amide (LSD) was bound by normal rabbit serum. Precipitation by saturated ammonium sulphate reduced the degree of binding from 14,884 CP=A bound to 455 cpm bound. Purification of the IgG fraction further reduced this to 284 cpm bound. Rifled anti-lysergyl antibody demonstrated a KAO of 7.7 x lOsM I and a heterogeneity index (a) of 0.699. The IgG fraction from which it was obtained possessed a AT(O of 3.5 x 105 M I and an (a) of U.704. There is no measurable inhibition of anti-lysergyl antibody binding to LSD at a tryptophan concentration of less than 71 mcM. Passive administration of hyperimmune antibody, or active immunization resulted in nearly total neutralization of the drug effect in mice measured by the poke and rear teats. The percentage of (3H)-LSD bound byantilysergyl IgG fraction was 100 % by purified anti - lysergyl antibody was 40.2% by adsorbed antilysergyl IgG fraction was 27.2% and by normal IgG was 0.36%. Conclusions Use of IgG fractions of antidrug sera permit measurement of heterogeneity and affinity without selective bias.
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