[Study of the receptor for black widow spider neurotoxin. II. Isolation and characteristics of the receptor from bovine brain membranes]. / Issledovanie retseptora neirotoksina pauka karakurta. II. Vydelenie i kharakteristika reteseptora iz membran mozga byka.

Biospecific sorbents for isolation of the latrotoxin receptor have been obtained and studied. Binding of the receptor components solubilized from the bovine cerebral cortex membrane to the immobilized toxin critically depends on the presence of calcium ions and the solution ionic strength. The procedure for semipreparative isolation of the highly active receptor preparation with Kd = 9 x 10(-10) M and Bmax = 0.9 nmol/mg has been developed. Binding activity of the isolated receptor is inhibited by heating as well as by proteases and denaturing agents. According to electrophoretic analysis in the presence of SDS the receptor complex contains protein components of molecular mass 200, 160, 79, 43 kDa, the former two being glycoproteins.

[Identification of the neuronal protein with antigenic properties of latrotoxin]. / Identifikatsiia neironal'nogo belka s antigennymi svoistvami latrotoksina.

Monospecific antibodies against neurotoxin from the black widow spider venom (alpha-latrotoxin) have been used to identify a neuronal protein (s) with latrotoxin-like epitopes. As determined by ELISA, the protein is localized in cytoplasmic fraction of bovine brain. It was partially purified by anion-exchange chromatography and preparative SDS-electrophoresis. Immunoblotting data indicate that this neuronal acidic protein has molecular mass of ca. 100 kDa.

[Purification of a soluble tetrodotoxin-sensitive protein from the cytoplasmic fraction of bovine brain tissue]. / Ochistka rastvorimogo tetrodotoksinchuvstvitel'nogo belka iz tsitoplazmicheskoi fraktsii tkani golovnogo mozga krupnogo rogatogo skota.

Highly purified protein inducing tetrodotoxin-dependent Na fluxes in liposomal membrane was obtained from the cytoplasmic fraction of the bovine brain. The protein was purified by anion-exchange chromatography on DEAE-Servacell and wheat germ agglutinin sepharose (WGA) followed by gel filtration on sepharose 4B. It is a high-molecular weight acidic glycoprotein; during denaturation under reducing conditions it forms 55 kD subunits. It is suggested that the tetrodotoxin-sensitive protein could be a soluble intracellular precursor of the voltage-dependent sodium channels.