Analysis of L-[3H]-glutamate radioligand binding to plasma membranes of the ampullae of Lorenzini of skates.
Radioligand binding analysis of L-[3H]-glutamate to plasma membranes of the ampullae of Lorenzini in the skate revealed one type of binding site with KD = 286 nM and Bmax = 2.1 pmol mg-1 protein. It was revealed that Na+, K+, Ca2+ and Mg2+ inhibited the L-[3H]-glutamate binding, while Cl- had no effect. The glutamate agonists kainate, quisqualate and N-methyl-D-aspartate (NMDA) were shown to inhibit glutamate binding in a dose-dependent manner. The results obtained confirm the electrophysiological observations suggesting the existence of three types of glutamate receptor at afferent synapses of the ampullae of Lorenzini of skates.
Akoev
G N
GN
Pavlov Institute of Physiology, Russian Academy of Sciences, St Petersburg.
Dambinova
S A
SA
Ryzhova
I V
IV
Gorodinsky
A I
AI
D000818:Animals; D002412:Cations / Q000494:pharmacology; D002462:Cell Membrane / Q000378:metabolism; D004594:Electrophysiology; D005971:Glutamates / Q000378:metabolism*; D018698:Glutamic Acid; D066298:In Vitro Techniques; D007608:Kainic Acid / Q000494:pharmacology; D016202:N-Methylaspartate / Q000494:pharmacology; D016318:Quisqualic Acid / Q000494:pharmacology; D017470:Receptors, Glutamate / Q000187:drug effects / Q000378:metabolism; D012860:Skates, Fish / Q000378:metabolism*; D013570:Synaptic Membranes / Q000187:drug effects / Q000378:metabolism
D002412:Cations; D005971:Glutamates; D017470:Receptors, Glutamate; D018698:Glutamic Acid; D016202:N-Methylaspartate; D016318:Quisqualic Acid; D007608:Kainic Acid