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. 1988 Dec 1;7(12):3717–3726. doi: 10.1002/j.1460-2075.1988.tb03255.x

Glycine receptor heterogeneity in rat spinal cord during postnatal development.

C M Becker 1, W Hoch 1, H Betz 1
PMCID: PMC454946  PMID: 2850172

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.

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Selected References

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