β-银环蛇毒素。[3H] 吡哆醛化β-银环蛇毒素与一种高分子量蛋白质受体的结合。
beta-Bungarotoxin. The binding of [3H]pyridoxylated beta-bungarotoxin to a high-molecular-weight protein receptor.
作者信息
MacDermot J, Westgaard R H, Thompson E J
出版信息
Biochem J. 1978 Oct 1;175(1):281-8. doi: 10.1042/bj1750281.
beta-Bungarotoxin was labelled with pyridoxal 5'-phosphate (incorporating 3H). The kinetics of beta-bungarotoxin binding to several tissue subfragments of nervous tissue was studied. The dissociation constant of 3H-pyridoxylated beta-bungarotoxin in this reaction was 0.21-0.37 micron and that of unlabelled beta-bungarotoxin was 25 nM. Hill [(1910) J. Physiol. (London) 40, iv-vii] and Scatchard [(1949) Ann. N.Y. Acad. Sci. 51, 660-672] analyses demonstrated no co-operativity of binding and only a single class of receptor sites, consistent with a bimolecular association of beta-bungarotoxin and its receptor. The iodinated toxin was physiologically inactive. Toxin was bound in non-specific unsaturable fashion by glass and/or plastic. This low-affinity binding was corrected by addition of bovine serum albumin to a final concentration of 30 mg/ml. A soluble protein receptor of beta-bungarotoxin was isolated and the mol.wt. is approx. 200000.
β-银环蛇毒素用5'-磷酸吡哆醛（含³H）进行标记。研究了β-银环蛇毒素与神经组织的几个组织亚片段结合的动力学。在该反应中，³H-吡哆醛化β-银环蛇毒素的解离常数为0.21 - 0.37微米，未标记的β-银环蛇毒素的解离常数为25纳摩尔。希尔[(1910)《生理学杂志》(伦敦)40, iv - vii]和斯卡查德[(1949)《纽约科学院学报》51, 660 - 672]分析表明不存在结合协同性，且只有一类受体位点，这与β-银环蛇毒素与其受体的双分子缔合一致。碘化毒素无生理活性。毒素以非特异性、不可饱和的方式与玻璃和/或塑料结合。通过添加终浓度为30毫克/毫升的牛血清白蛋白可校正这种低亲和力结合。分离出了β-银环蛇毒素的可溶性蛋白受体，其分子量约为200000。
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