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作 者:王银[1,2] 徐科[1,2] 沈国光 杜晓燕[1,2] 周元聪
机构地区:[1]中国科学院上海生理研究所 [2]中国科学院上海生物化学研究所
出 处:《Zoological Research》1998年第6期429-433,共5页动物学研究(英文)
基 金:国家自然科学基金
摘 要:以加州电鳐(Torpedocalifornica)电器官为材料,探索了用去垢剂TritonX-100增溶抽提β-蝮蛇毒素(βagkistrodotoxin,βAgTX)结合蛋白的合适条件,建立了此结合蛋白活性的检测方法,并分析了该结合蛋白与同位素125I标记βAgTX的结合性质。结果显示这种电器官中存在相对含量较高的毒素结合位点,其密度为1580fmoL/mg蛋白质,此结合作用的平衡解离常数KD值为55×10-9mol/L。去垢剂TritonX-100可以有效地将该结合蛋白从电器官组织膜上增溶下来,抽提效率接近50%,为分离、纯化此结合蛋白建立了基础。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.
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