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Antibodies Against the Bovine Brain Glutamate Binding Protein
Author(s) -
Roy Sabita,
Michaelis Elias K.
Publication year - 1984
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.1471-4159.1984.tb02757.x
Subject(s) - antibody , glutamate dehydrogenase , glutamate receptor , glutamine synthetase , enzyme , glutamate decarboxylase , glutamine , biochemistry , microbiology and biotechnology , chemistry , biology , amino acid , immunology , receptor
Antibodies against the purified bovine brain glutamate binding protein (GBP) were raised in rabbits. Both nonderivatized and dinitrobenzene‐derivatized GBP produced strong immunological responses in rabbits. Using the enzyme‐linked immunosorbent assay (ELISA), we have quantified the antibody production and determined the specificity of the antibodies. Bovine brain GBP and the analogous protein from rat brain interacted most strongly with the antibodies. A bacterial glutamate‐aspartate binding protein, as well as the enzymes glutamate dehydrogenase (EC 1.4.1.3), glutamine synthetase (EC 6.3.1.2), and γ‐glutamyl transpeptidase (EC 2.3.2.2), showed little or no cross‐reactivity with the anti‐GBP antibodies. A crude bacterial glutamate decarboxylase (EC 4.1.1.15) preparation gave a small to moderate cross‐reaction with the anti‐GBP antibodies. The sensitivity of the ELISA assay and the specificity of the antibodies were such that GBP levels as low as 3–10 ng could be detected.