Andres R Y, Jeng I, Bradshaw R A
Proc Natl Acad Sci U S A. 1977 Jul;74(7):2785-9. doi: 10.1073/pnas.74.7.2785.
Two classes of receptors for 125I-labeled nerve growth factor in chick embryonic dorsal root neurons have been observed. One type is associated with the plasma membrane (or microsomal fraction) and can be completely solubilized by Triton X-100. These receptors display the nonsaturable binding isotherms and curvilinear Scatchard plots previously reported for nerve growth factor receptors in whole cells. The second class of binding sites is located in the nucleus, firmly bound to chromatin. These receptors are not solubilized by detergent, show saturable binding, and yield linear Scatchard plots of the type associated with a single class of binding sites of high affinity. The presence of the two receptor types suggests a bimodal mechanism of action for nerve growth factor.
在鸡胚背根神经元中观察到了两类针对¹²⁵I标记神经生长因子的受体。一类与质膜（或微粒体部分）相关，可被Triton X - 100完全溶解。这些受体呈现出先前报道的全细胞中神经生长因子受体的非饱和结合等温线和曲线形Scatchard图。第二类结合位点位于细胞核内，与染色质紧密结合。这些受体不能被去污剂溶解，表现出饱和结合，并产生与一类高亲和力单一结合位点相关的线性Scatchard图。两种受体类型的存在提示了神经生长因子的双模态作用机制。
