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神经丝蛋白在鱿鱼巨轴突中发生磷酸化。

Neurofilament protein is phosphorylated in the squid giant axon.

作者信息

Pant H C, Shecket G, Gainer H, Lasek R J

出版信息

J Cell Biol. 1978 Aug;78(2):R23-7. doi: 10.1083/jcb.78.2.r23.

DOI:10.1083/jcb.78.2.r23

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2110134/

Abstract

We have observed the phosphorylation of neurofilament protein from squid axoplasm. Phosphorylation is demonstrated by 32P labeling of protein during incubation of axoplasm with [gamma-32P]ATP. When the labeled proteins are separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), two bands, at 2.0 x 10(5) daltons and greater than 4 x 10(5) daltons, contain the bulk of the 32P. The 2.0 x 10(5)-dalton phosphorylated polypeptide comigrates on SDS-PAGE with one of the subunits of squid neurofilament protein. Both major phosphorylated polypeptides co-fractionate with neurofilaments in discontinuous sucrose gradient centrifugation and on gel filtration chromatography on Sepharose 4B. The protein-phosphate bond behaves like a phospho-ester, and labeled phospho-serine is identified in an acid hydrolysate of the protein. The generality of this phenomenon in various species and its possible physiological significance are discussed.

摘要

我们观察到了鱿鱼轴浆中神经丝蛋白的磷酸化。在轴浆与[γ-32P]ATP孵育期间，通过蛋白质的32P标记来证明磷酸化。当通过SDS-聚丙烯酰胺凝胶电泳（SDS-PAGE）分离标记的蛋白质时，两条带，分别为2.0×10（5）道尔顿和大于4×10（5）道尔顿，含有大部分的32P。2.0×10（5）道尔顿的磷酸化多肽在SDS-PAGE上与鱿鱼神经丝蛋白的一个亚基共迁移。在不连续蔗糖梯度离心和Sepharose 4B凝胶过滤色谱中，两种主要的磷酸化多肽都与神经丝共分级分离。蛋白质-磷酸键表现得像磷酸酯，并且在蛋白质的酸水解产物中鉴定出标记的磷酸丝氨酸。讨论了这种现象在各种物种中的普遍性及其可能的生理意义。