Gurd J W
Brain Res. 1985 May 6;333(2):385-8. doi: 10.1016/0006-8993(85)91599-9.
Incubation of postsynaptic densities (PSDs) with [gamma-32P]adenosine triphosphate (ATP) results in the phosphorylation of a number of proteins. Of these, phosphoproteins with apparent molecular weights (Mr) of 51,000, 180,000, 300,000, 320,000 and 370,000 contain 32P which is resistant to digestion with hot KOH suggesting the presence of [32P]phosphotyrosine residues. Phosphoamino acid analysis of total 32P-labelled PSDs identified [32P]phosphotyrosine as well as phosphoserine and phosphothreonine as products of the phosphorylation reaction. The PSD-specific glycoprotein gp180 was isolated from 32P-labelled PSDs and shown to contain [32P]phosphotyrosine. The results identify tyrosine kinase as a component of purified PSDs and gp180 as an endogenous substrate for this enzyme.
用[γ-32P]三磷酸腺苷（ATP）孵育突触后致密物（PSD）会导致多种蛋白质发生磷酸化。其中，表观分子量（Mr）为51,000、180,000、300,000、320,000和370,000的磷蛋白含有32P，该32P对热KOH消化具有抗性，表明存在[32P]磷酸酪氨酸残基。对总32P标记的PSD进行磷酸氨基酸分析，确定[32P]磷酸酪氨酸以及磷酸丝氨酸和磷酸苏氨酸为磷酸化反应的产物。从32P标记的PSD中分离出PSD特异性糖蛋白gp180，并显示其含有[32P]磷酸酪氨酸。这些结果确定酪氨酸激酶是纯化的PSD的一个组成部分，并且gp180是该酶的内源性底物。
