Rusenko K W, Stach R W
Neurochem Res. 1981 Mar;6(3):287-300. doi: 10.1007/BF00964044.
We have demonstrated that the beta nerve growth factor will interact with various acidic proteins apparently nonspecifically. When 125I-labeled beta nerve growth factor at a concentration of 3.8 X 10(-10) M is incubated with an acidic protein at 2 mg/ml (4.5 X 10(-6)-4.4 X 10(-5) M), a complex is formed. This complex changes the isoelectric point of the 125I-labeled beta nerve growth factor sufficiently so that the 125I-labeled beta nerve growth factor migrates anomalously in polyacrylamide gel electrophoresis. The interaction between beta nerve growth factor and bovine serum albumin, which appears to be complex, may be the cause of the previously reported activation of the beta nerve growth factor when bovine serum albumin is present in a typical bioassay.
我们已经证明,β神经生长因子会与各种酸性蛋白发生明显的非特异性相互作用。当浓度为3.8×10⁻¹⁰ M的¹²⁵I标记的β神经生长因子与浓度为2 mg/ml(4.5×10⁻⁶ - 4.4×10⁻⁵ M)的酸性蛋白一起孵育时,会形成一种复合物。这种复合物足以改变¹²⁵I标记的β神经生长因子的等电点,使得¹²⁵I标记的β神经生长因子在聚丙烯酰胺凝胶电泳中出现异常迁移。β神经生长因子与牛血清白蛋白之间的相互作用似乎很复杂,这可能是先前报道的在典型生物测定中存在牛血清白蛋白时β神经生长因子被激活的原因。