title: Chick kainate binding protein lacks GTPase activity.
abstract: Chick kainate binding protein was solubilized from cerebellar membranes and purified (x19) by use of two chromatographic steps. Measurements of [3H]kainate binding and GTPase activity in the different fractions reveal a consistent decrease of GTPase activity as the purification proceeds so that no GTPase is detectable after the final purification step. This fact, in the context of the differential involvement in nucleotide recognition of some critical amino acid residues in the p-loop motif of GTPases and in the guanine nucleotide-binding sequence of ionotropic glutamate receptors, together with significant discrepancies concerning the activity of individual nucleotides, suggests that both guanine nucleotide-recognizing sequences are unlikely to be alternative expressions of the same functional domain.
authors.affiliation: Departamento de Bioquímica, CCB, Universidade Federal de Santa Catarina, Florianópolis, Brazil.
authors.forename: C I
authors.initials: CI
authors.lastname: Tasca
authors.forename: J S
authors.initials: JS
authors.lastname: Burgos
authors.forename: A
authors.initials: A
authors.lastname: Barat
authors.forename: D O
authors.initials: DO
authors.lastname: Souza
authors.forename: G
authors.initials: G
authors.lastname: Ramírez
mesh_terms: D000818:Animals; D001667:Binding, Competitive; D002531:Cerebellum / Q000737:chemistry / Q000201:enzymology*; D002645:Chickens; D003208:Concanavalin A; D003568:Cytidine Monophosphate / Q000378:metabolism; D004983:Ethanolamines; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D018092:Kainic Acid Receptors / Q000302:isolation & purification / Q000378:metabolism*; D012685:Sepharose; D014316:Tritium
chemical_list: D003208:Concanavalin A; D003568:Cytidine Monophosphate; D004983:Ethanolamines; D020558:GTP Phosphohydrolases; D018092:Kainic Acid Receptors; D012685:Sepharose; D014316:Tritium; C007369:2-diethylaminoethanol