Harris-Warrick R M, Bothwell M A, Shooter E M
J Biol Chem. 1980 Dec 10;255(23):11284-9.
The binding of the beta nerve growth factor subunit in the 7 S nerve growth factor complex to the two nerve growth factor receptors on chick embryo dorsal root ganglion cells was investigated. Under conditions where the 7 S nerve growth factor complex is maximally stable (in the presence of excess alpha and gamma subunits and of 20 to 30 microM zinc ion), no binding to either receptor was detectable. The time course of the decrease in the binding of beta nerve growth factor to the receptors upon addition of alpha and gamma subunits and zinc ion paralleled the formation of the 7 S complex. Addition of alpha and gamma subunits and zinc ion to the bisdes-arginine118-nerve growth factor, which does not re-form the 7 S complex, failed to inhibit the binding of the derivative to either receptor. While the alpha subunit alone had no effect on beta nerve growth factor binding, the gamma subunit decreased its binding in proportion to the amount of complex formed between these two subunits, suggesting that the beta . gamma complex, like the 7 S complex, does not bind to nerve growth factor receptors.
研究了7S神经生长因子复合物中的β神经生长因子亚基与鸡胚背根神经节细胞上两种神经生长因子受体的结合情况。在7S神经生长因子复合物最大程度稳定的条件下（存在过量的α和γ亚基以及20至30微摩尔锌离子），未检测到与任何一种受体的结合。加入α和γ亚基以及锌离子后，β神经生长因子与受体结合减少的时间进程与7S复合物的形成平行。向不能重新形成7S复合物的双去精氨酸118 - 神经生长因子中加入α和γ亚基以及锌离子，未能抑制该衍生物与任何一种受体的结合。虽然单独的α亚基对β神经生长因子的结合没有影响，但γ亚基以与这两个亚基之间形成的复合物量成比例的方式降低其结合，这表明β.γ复合物与7S复合物一样，不与神经生长因子受体结合。
