Glycine receptor heterogeneity in rat spinal cord during postnatal development.
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.
Becker
C M
CM
Zentrum für Molekulare Biologie, Universität Heidelberg, FRG.
Hoch
W
W
Betz
H
H
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D015153:Blotting, Western; D002499:Centrifugation, Density Gradient; D008970:Molecular Weight; D011233:Precipitin Tests; D051381:Rats; D018009:Receptors, Glycine; D017981:Receptors, Neurotransmitter / Q000302:isolation & purification / Q000502:physiology*; D013116:Spinal Cord / Q000254:growth & development* / Q000502:physiology
D000911:Antibodies, Monoclonal; D018009:Receptors, Glycine; D017981:Receptors, Neurotransmitter