- 作者: Yi-Hsuan Lee; Ken Schmidt; David L. Deupree; Jang-Yen Wu
- 作者服務機構: Department of Physiology and Cell Biology, University of Kansas, Lawrence, Kans., USA
- 中文摘要: --
- 英文摘要: A high-molecular-weight glutamate-binding inhibitor (HGBI) from porcine brain extract was purified to homogeneity. The results of this purification pro- cess show that glutamate receptor activity can be regulated by a high-molecu- lar-weight protein, which inhibits [3H]L-glutamate binding to excitatory ami- no acid (EAA) receptors. The purified HGBI appears to be a protein with a molecular weight of approximately 70 kD. The purified HGBI is negatively charged, suggesting that it may contain acidic amino acids, and most likely, L-glutamate- and L-aspartate-enriched regions, responsible for its surface charge as well as for its binding to glutamate receptors. Inhibition of [3H]L- glutamate binding by the purified HGBI is reversible, and appears to change the binding kinetics. This endogenous ligand for glutamate receptors has unique characteristics separating it from all the other ligands found so far in the EAA receptor system. This HGBI represents a new class of modulator for the EAA receptor, thus further investigation of the function and structure of the HGBI should provide new understanding of the mechanisms of EAA- mediated neurotransmission.
- 中文關鍵字: --
- 英文關鍵字: Endogenous glutamate modulator; Protein purification; Excitatory amino acids