Solubilization of β-Agkistrodotoxin-Binding Protein From Torpedo Electric Organ and Studies on Its Binding Properties With the Toxin

WANG Yin; XU Ke; SHEN Guo-guang; DU Xiao-yan; ZHOU Yuan-cong

Volume 19 Issue 6

Nov. 1998

Turn off MathJax

Article Contents

Article Navigation > Zoological Research > 1998 > 19(6): 429-433

WANG Yin, XU Ke, SHEN Guo-guang, DU Xiao-yan, ZHOU Yuan-cong. Solubilization of β-Agkistrodotoxin-Binding Protein From Torpedo Electric Organ and Studies on Its Binding Properties With the Toxin. Zoological Research, 1998, 19(6): 429-433.

Citation:

PDF( 143 KB)

Solubilization of β-Agkistrodotoxin-Binding Protein From Torpedo Electric Organ and Studies on Its Binding Properties With the Toxin

1.
Shanghai Institute of Physiology,the Chinese Academy of Sciences,Shanghai 200031 2.Shanghai Institute of Biochemistry,the Chinese Academy of Sciences,Shanghai 200031

Received Date: 1900-01-01
Rev Recd Date: 1900-01-01
Publish Date: 1998-12-22

Abstract

Abstract

It was infered that β-agkistrodotoxin-binding protein is presumably a novel presynaptic functional protein involved in neurotransmitter release.This paper reported studies on solubilization of β-agkistrodotoxin-binding protein from Torpedo californica electric organ,a tissue rich in synapses.The binding assay of this protein was established using a PEG precipitation method,and its binding properties with [125]I labelled β-AgTX was preliminarily determined.The results showed that the density of β-AgTX-binding sites in this tissue is relatively high (much higher than that of rat brain).B[max] is 1580 fmol/mg protein and K[D] value is 5.5×10[-9] mol/L.Triton X-100 was proved an effective detergent for the extraction experiment with a yield of about 50%.Thus a hopeful beginning for isolation and purification of β-agkistrodotoxin-binding protein was accomplished.
- β-AgTX-binding protein,
- Solubilization,
- Torpedo electric organ