Chick Kainate Binding Protein Lacks Gtpase Activity
NEUROREPORT(1999)
Abstract
CHICK kainate binding protein Nas solubilized from cerebellar membranes and purified (X19) by use of two chromatographic steps. Measurements of [H-3]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. NeuroReport 10:1981-1983 (C) 1999 Lippincott Williams & Wilkins.
MoreTranslated text
Key words
chick kainate binding protein,guanine nucleotides,GMP,GTPases,ionotropic glutamate receptors,p-loop
AI Read Science
Must-Reading Tree
Example
![](https://originalfileserver.aminer.cn/sys/aminer/pubs/mrt_preview.jpeg)
Generate MRT to find the research sequence of this paper
Chat Paper
Summary is being generated by the instructions you defined