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Extracts from the rat brain were screened to identify a putative endogenous ligand for the binding sites of the neuroexcitant kainic acid (KA). The extracted substances were separated by chromatographic techniques and tested for their ability to inhibit KA binding to fish synaptosomes and to membranes from rat brain. A substance isolated in this way (rat kainate-binding inhibitor, RKBI) display a competitive interaction with KA for the low-affinity binding sites in rat brain membranes. According to the separation behavior in the purification step, RKBI is distinct from an inhibitor formerly isolated from fish nervous tissue (KBI). The substance exhibits positive co-operativity with KA for a very-low-affinity site population, particularly concentrated in the cerebellum, and could play a physiological role in this area.
P Migani, and
E Ciani, and
M Virgili, and
O Barnabei
January 1986,
Advances in experimental medicine and biology,
P Migani, and
E Ciani, and
M Virgili, and
O Barnabei
December 1987,
Journal of steroid biochemistry,
P Migani, and
E Ciani, and
M Virgili, and
O Barnabei
December 1986,
Journal of biochemistry,
P Migani, and
E Ciani, and
M Virgili, and
O Barnabei
July 1993,
Neuroscience letters,
P Migani, and
E Ciani, and
M Virgili, and
O Barnabei
January 1988,
Annals of the New York Academy of Sciences,
P Migani, and
E Ciani, and
M Virgili, and
O Barnabei
July 1980,
European journal of pharmacology,
P Migani, and
E Ciani, and
M Virgili, and
O Barnabei
July 1984,
Endocrinology,
P Migani, and
E Ciani, and
M Virgili, and
O Barnabei
July 2001,
British journal of pharmacology,
P Migani, and
E Ciani, and
M Virgili, and
O Barnabei
May 1988,
The Journal of biological chemistry,
P Migani, and
E Ciani, and
M Virgili, and
O Barnabei
February 2003,
Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie,
