Campistron G, Geffard M, Buijs R M
J Neurochem. 1986 Mar;46(3):862-8. doi: 10.1111/j.1471-4159.1986.tb13051.x.
An immunological approach to the detection of taurine resulted in antibodies specific enough to be used for immunocytochemical studies. The experimental conditions were similar to those previously described for raising antibodies against some small-sized neurotransmitter molecules: antisera were obtained from rabbits immunized with taurine conjugated to carrier proteins via glutaraldehyde and purified by adsorption on the glutaraldehyde-treated protein carriers. Antibody affinity and specificity were determined in competition experiments between conjugated taurine and other conjugated amino acids or derivatives by enzyme-linked immunosorbent assay. The resulting cross-reactivity ratios, calculated at half-displacement, showed conjugated taurine to be the best recognized compound. Given the molecular structure of taurine and the method used to prepare the conjugate, it seemed necessary to perform an oxidation step. However, adsorption of antisera on reoxidized or nonreoxidized taurine conjugates suggested that reoxidation did not make a significant difference. Immunocytochemical application of the sera revealed populations of strongly immunopositive nerve cells in the cerebellum, striatum, and septum. The results confirmed that antitaurine antibodies can be used as specific tools for a better understanding of the role of taurine in the central nervous system.
