A protein complex that exhibited-properties of an ionotropic glutamate rece
ptor was isolated from locust muscles. A one-step biospecific chromatograph
y on a sorbent with the immobilized polyamine toxins from spider venom (arg
iopinins) was used for its isolation. The resulting preparation was capable
of specific binding of L-[H-3] glutamic (K-d 0.47 mu M, B-max 2300 pmol/mg
) and [H-3]-L-aspartic acids (K-d 0.65 mu M, B-max 1870 pmol/mg). Three sub
types of glutamate receptors characteristic of the locust muscle tissues we
re found in the preparation.