Kainyl-bovine serum albumin: a novel ligand of the kainate sub-type of glutamate receptor with a very high binding affinity
| Autor: | Gerardo Lederkremer, Paul Gregor, Ora Goldberg, Vivian I. Teichberg, Antoine Triller, Michel Beaujean, Arturo Ortega, Nomi Eshhar |
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| Předmět: |
Glycine
Serum albumin Kainate receptor Binding Competitive Cerebellum Goldfish Mole Animals Binding site Bovine serum albumin Molecular Biology Kainic Acid biology General Neuroscience Glutamate receptor Brain Rats Inbred Strains Ligand (biochemistry) Rats Receptors Neurotransmitter Dissociation constant Kinetics Receptors Glutamate Biochemistry biology.protein Rabbits Neurology (clinical) Chickens Subcellular Fractions Developmental Biology |
| Zdroj: | Europe PubMed Central |
| Popis: | Bovine serum albumin has been conjugated with kainylaminooxyacetylglycine to afford a multivalent kainylated protein called kainyl-bovine serum albumin (KA-BSA). This derivative, radiolabelled with 125I to more than 5000 Ci/mmol, was found to interact in the chick, goldfish and rat brain to specific membranous sites displaying the pharmacological properties attributed to the kainate sub-type of glutamate receptor. Measurements of the kinetics of association and dissociation of KA-BSA showed a quasi-irreversible binding with dissociation constants in the subpicomolar and nanomolar range. The chemical properties and the binding characteristics of KA-BSA suggest that it interacts mainly with kainate binding sites present in clusters in the membrane. Localization of the KA-BSA binding sites, by autoradiography in the chick cerebellum and by immunoperoxidase staining in the goldfish cerebellum, revealed an exclusive association with the molecular layer. |
| Databáze: | OpenAIRE |
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