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Glycine receptor heterogeneity in rat spinal cord during postnatal development.
Author(s) -
Becker C. M.,
Hoch W.,
Betz H.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb03255.x
Subject(s) - glycine receptor , biology , strychnine , receptor , glycine , gene isoform , antigenicity , postsynaptic potential , protein subunit , spinal cord , ligand (biochemistry) , microbiology and biotechnology , biochemistry , antibody , amino acid , immunology , neuroscience , gene
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.