Solubilization of the glycine receptor from rat spinal cord

Brain ResearchPublished 1 December 1981

Friedhelm Pfeiffer, Heinrich Betz

DOI10.1016/0006-8993(81)91099-4

Source URL

Citations81

SJR quartileQ2

SJR score0.85

SNIP0.72

TL;DR

Abstract

Glycine receptors, as detected by glycine-displaceable [3H]strychnine binding, were solubilized from a membrane fraction of rat spinal cord by the non-ionic detergent Triton X-100. The solubilized material retained its high affinity for [3H]strychnine and exhibited the typical pharmacological properties of the membrane-bound glycine receptor. On sucrose density gradients, the solubilized receptor had a sedimentation coefficient of 8.3 +/- 0.4 S. Gel exclusion chromatography on Sepharose 6 B in the presence of phosphatidylcholine gave a Stokes radius of 7.3 +/- 0.3 nm.

Keywords

NeuroscienceBiochemistry, Genetics and Molecular Biology

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An analysis has been made in anaesthetised cats of the depression by glycine and related amino acids of the firing of spinal dorsal horn interneurones, Renshaw cells and cortical neurones, and the involvement of a glycine-like amino acid as a major spinal inhibitory transmitter is discussed.

Experimental Brain ResearchThe hyperpolarization of spinal motoneurones by glycine and related amino acids

483 Citations1968D.R. Curtis, L. H�sli +2 more

The results indicate that glycine may be a major spinal inhibitory transmitter, in which case strychnine affects spinal postsynaptic inhibition by limiting the action of glycine upon subsynaptic inhibitory receptors.

Proceedings of the National Academy of SciencesStrychnine Binding Associated with Glycine Receptors of the Central Nervous System

389 Citations1973Anne B. Young, Solomon H. Snyder

The regional localization of strychnine binding in the central nervous system correlates closely with endogenous glycine concentrations, and in subcellular fractionation experiments, stryhnine binding is most enhanced in synaptic-membrane fractions.

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Molecular PharmacologyStrychnine Binding in Rat Spinal Cord Membranes Associated with the Synaptic Glycine Receptor: Cooperativity of Glycine Interactions

172 Citations1974Anne B. Young, Solomon H. Snyder

Glycine and strychnine appear to bind to distinct sites which interact in a cooperative fashion, while Detergents such as deoxycholate and Triton X-100 decrease receptor binding in concentrations which solubilize membrane protein.

Proceedings of the National Academy of SciencesThe Glycine Synaptic Receptor: Evidence That Strychnine Binding Is Associated with the Ionic Conductance Mechanism

136 Citations1974Anne B. Young, Solomon H. Snyder

The ability of a series of anions to inhibit strychnine binding to spinal cord synaptic membranes correlates closely with their neurophysiologic capacity to reverse inhibitory postsynaptic potentials in the mammalian spinal cord.

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Analytical BiochemistryLowry assay of dilute protein solutions containing high concentrations of Triton X-100

71 Citations1975Jesudian ChandraRajan, LeRoy Klein

Two simple procedures are presented for the Lowry assay of dilute protein samples containing 1–5% Triton X-100, which could reduce interference to an insignificant level either by centrifuging the precipitate and incorporating Tritons X- 100 in both the reagent blank and standards, or by removing the detergent prior to the assay.