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Antisera Against the Indolealkylamines: Tryptophan, 5‐Hydroxytryptophan, 5‐Hydroxytryptamine, 5‐Methoxytryptophan, and 5‐Methoxytryptamine Tested by an Enzyme‐Linked Immunosorbent Assay Method
Author(s) -
Geffard Michel,
Dulluc Josette,
Rock AnneMarie
Publication year - 1985
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1985.tb08747.x
Subject(s) - antiserum , glutaraldehyde , conjugate , tryptophan , enzyme , bovine serum albumin , 5 hydroxytryptophan , antibody , chemistry , biochemistry , serum albumin , cross reactivity , lysine , conjugated system , albumin , microbiology and biotechnology , serotonin , biology , cross reactions , chromatography , immunology , amino acid , organic chemistry , mathematical analysis , receptor , mathematics , polymer
Antisera were raised against tryptophan, 5‐hydroxytryptophan, 5‐hydroxytryptamine, 5‐methoxytryptophan, and 5‐methoxytryptamine, by conjugating each molecule to bovine serum albumin and to human serum albumin via glutaraldehyde, in such a way as to preserve the original part. Antibody specificity was tested with the enzyme‐linked immunosorbent assay method. The specificity of each anti‐indolealkylamine‐glutaraldehyde antibody was established with competition experiments by using an adsorbed immunogenic conjugate and indolealkylamines either free or conjugated with poly‐L‐lysine. The nonconjugated compounds were poorly recognized. In the same way, the nonreduced conjugates always appeared less immunoreactive than the reduced ones. Calculated from the specificity study of each antiserum, the cross‐reactivity ratios were found to be smallest for the most immunoreactive conjugates. Thus, a specific immune response was defined for each compound belonging to the same metabolic pathway.