Glycine receptor heterogeneity in rat spinal cord during postnatal development

EMBO J. 1988 Dec 1;7(12):3717-26.

Abstract

Two different isoforms of the inhibitory glycine receptor were identified during postnatal development of rat spinal cord. A neonatal form characterized by low strychnine binding affinity, altered antigenicity, and a ligand binding subunit differing in mol. wt (49 kd) from that of the adult receptor (48 kd) predominates at birth (70% of the total receptor protein). Separation from the adult form could be achieved by either use of a selective antibody or glycine gradient elution of 2-aminostrychnine affinity columns. Both isoforms co-purify with the mol. wt 93 kd peripheral membrane protein of the postsynaptic glycine receptor complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology
  • Blotting, Western
  • Centrifugation, Density Gradient
  • Molecular Weight
  • Precipitin Tests
  • Rats
  • Receptors, Glycine
  • Receptors, Neurotransmitter / isolation & purification
  • Receptors, Neurotransmitter / physiology*
  • Spinal Cord / growth & development*
  • Spinal Cord / physiology

Substances

  • Antibodies, Monoclonal
  • Receptors, Glycine
  • Receptors, Neurotransmitter