3022866

Presence of a highly efficient "binding" to bacterial contamination can distort data from binding studies.

Article date: 1990/12/1

PubMed ID: 3022866

Journal name: Neurochemical research (ISSN: 0364-3190)

ABSTRACT

[3H]GABA at low concentrations (5-10 nM) was bound by what appeared to be a “GABA receptor binding site” in bacterial contamination originating from a batch of distilled water. Under experimental conditions similar to those usually employed in [3H]GABA binding studies, the apparent binding displayed a very high “specific” component and a high efficiency in terms of [3H]GABA bound per mg of protein. The “binding” was blocked by muscimol but not by isoguvacine, SR95531 and nipecotic acid. These characteristics suggest that the presence of such spurious binding in the experiments using 3H-labeled ligands in brain homogenates may not always be very obvious and, moreover, it can result in subtle, but serious, distortions of data from such studies, which may not be immediately recognized.

Author List: Balcar V J

Publication Types: Journal Article

Substances mentioned in the article: GABA Antagonists; Isonicotinic Acids; Nipecotic Acids; Pyridazines; Receptors, GABA-A; Tritium; nipecotic acid; Muscimol; gamma-Aminobutyric Acid; gabazine; Proline; homoproline; isoguvacine;

Mesh terms: Animals; Cats; Cerebral Cortex/metabolism; GABA Antagonists; Gram-Positive Bacteria/isolation & purification; Isonicotinic Acids/pharmacology; Muscimol/pharmacology; Nipecotic Acids/pharmacology; Proline/analogs & derivatives; Pyridazines/pharmacology; Radioligand Assay; Receptors, GABA-A/analysis; Tritium; gamma-Aminobutyric Acid/metabolism;

Citations: - GABAergic inactivation of the central pattern generators for locomotion in isolated neonatal rat spinal cord.

3022866.txt · Last modified: 2018/11/20 14:26 (external edit)