Pant H C, Yoshioka T, Tasaki I, Gainer H
Brain Res. 1979 Feb 23;162(2):303-13. doi: 10.1016/0006-8993(79)90291-9.
In vitro and in situ (after intracellular infusion) incubation of axoplasm from the squid giant axon with [gamma-32P]ATP produces a phosphorylation of primarily two proteins (of mol.wt. 200,000 and greater than 400,000). The phosphorylation of these proteins is stimulated by Mg2+, inhibited by Ca2+, and unaffected by 10(-7) to 10(-5) M cyclic nucleotides. The 200 kdalton and greater than 400 kdalton phosphorylated peaks appear to be neurofilament proteins, and phosphorylation of these peaks in situ is decreased by electrical stimulation of the axon.
用[γ-32P]ATP对鱿鱼巨轴突的轴浆进行体外和原位（细胞内注入后）孵育，主要产生两种蛋白质（分子量分别为200,000和大于400,000）的磷酸化。这些蛋白质的磷酸化受Mg2+刺激，受Ca2+抑制，且不受10(-7)至10(-5)M环核苷酸的影响。200千道尔顿和大于400千道尔顿的磷酸化峰似乎是神经丝蛋白，轴突的电刺激会使原位这些峰的磷酸化减少。
