Abstract
A specific binding protein to Joro spider toxin (JSTX) was isolated from the membranous fraction of bovine brain. The protein shows a molecular weight approximately 60±2K by SDS-PAGE and possesses a high affinity for JSTX. The possible role of the inhibitory action of JSTX may involve Ca dynamics in synaptic transmi ssion by NMDA, since the toxin selectively inhibits NMDA-derived Ca elevation in cultured hippocampal cells, and the amino acid sequence of the N-terminal portion of the toxin binding protein is homologous to calreticulin.
