Kainyl-bovine serum albumin: a novel ligand of the kainate subtype of glutamate receptor with a very high binding affinity

Nomi Eshhar, Gerardo Lederkremer, Michel Beaujean, Ora Goldberg, Paul Gregor, Arturo Ortega, Antoine Triller, Vivian I. Teichberg*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)57-70
Number of pages14
JournalBrain Research
Volume476
Issue number1
DOIs
StatePublished - 2 Jan 1989
Externally publishedYes

Keywords

  • Autoradiography
  • Chick cerebellum
  • Kainate receptor
  • Kainyl-bovine serum albumin
  • Ligand binding

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