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去污剂增溶的交感神经节神经生长因子受体的结合特性及表观分子大小

Binding characteristics and apparent molecular size of detergent solubilized nerve growth factor receptor of sympathetic ganglia.

作者信息

Costrini N V, Bradshaw R A

出版信息

Proc Natl Acad Sci U S A. 1979 Jul;76(7):3242-5. doi: 10.1073/pnas.76.7.3242.

Abstract

Nerve growth factor (NGF), a hormone-like regulator of sympathetic neuron ontogeny and metabolism affects its target cells initially by associating with specific plasma membrane receptors. We have solubilized the NGF receptor of adult rabbit superior cervical ganglia (SCG) with the nonionic detergent Triton X-100. The high-affinity equilibrium binding constant of the detergent-extracted receptor is 2-8 x 10(-10) M. Gel chromatography of the receptor or the 125I-labeled NGF receptor complex on a column of Sepharose 6B indicated, in both cases, a single component of an apparent hydrodynamic radius of 71 +/- 5 A. In parallel investigations, we have confirmed the similarity between the hydrodynamic size of the NGF receptor of rabbit SCG and that of the insulin receptor of IM-9 lymphocytes evaluated by similar methods.

摘要

神经生长因子(NGF)是一种对交感神经元个体发育和新陈代谢起激素样调节作用的物质,它最初通过与特定的质膜受体结合来影响其靶细胞。我们用非离子去污剂 Triton X - 100 溶解了成年兔颈上神经节(SCG)的 NGF 受体。去污剂提取的受体的高亲和力平衡结合常数为 2 - 8×10⁻¹⁰ M。在 Sepharose 6B 柱上对受体或¹²⁵I 标记的 NGF 受体复合物进行凝胶色谱分析,在两种情况下均显示出单一成分,其表观流体动力学半径为 71±5 Å。在平行研究中,我们通过类似方法证实了兔 SCG 的 NGF 受体的流体动力学大小与 IM - 9 淋巴细胞胰岛素受体的流体动力学大小相似。

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本文引用的文献

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Nerve growth factor and insulin.神经生长因子与胰岛素。
Science. 1972 May 5;176(4034):482-8. doi: 10.1126/science.176.4034.482.

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