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Solubilization of #beta#-bungarotoxin-binding protein from rat diaphragm and inhibition of its binding by some other presynaptic neurotoxins

Shen Guoguang, Zhuo Xiaoliang, Zhang Xinmei, Xu Ke

Shanghai Institute of Physiology, Chinese Academy of Sciences. Shanghai 200031

Abstract

This paper reports the solubilization of #beta#-bungarotoxin- binding protein from rat diaphragm membrane preparations with Triton X-100. The specific binding activities of the detergent extracts are 200-400 fmol/mg of protein, and the yields are about 50%-70%. The binding of ~(125)I-#beta#-bungarotoxin to the extracts could be completely inhibited by dendrotoxin, with an IC_(50) of about 8×10~(-8) mol/L. Another #beta#-agkistrodotoxin, however, could not inhibit the ~(125)I-#beta#-bungarotoxin binding at all. This indicates that the acting sites of #beta#-agkistrodotoxin on the presynaptic membranes are different from those of #beta#-bungarotoxin.

Key words: #beta#-bungarotoxin;#beta#-bungarotoxin-binding protein #beta#-agkistrodotoxin;Dendrotoxin;Ratdiaphragm;;

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Citing This Article：

Shen Guoguang, Zhuo Xiaoliang, Zhang Xinmei, Xu Ke. Solubilization of #beta#-bungarotoxin-binding protein from rat diaphragm and inhibition of its binding by some other presynaptic neurotoxins. Acta Physiol Sin 1996; 48 (1): (in Chinese with English abstract).