Innami T, Miyake M, Kakimoto Y
Neurosci Res. 1986 Dec;4(2):143-51. doi: 10.1016/0168-0102(86)90043-x.
During a study to find natural substrate proteins of carboxymethylation, myelin basic protein was found to be a good substrate. The two protein carboxymethylases were purified partially using myelin basic protein as a substrate. These two enzymes may be identical with protein carboxymethylase I and II, which have been found to methylate gamma-globulin. The Km of myelin basic protein (25 microM) was very small compared with other substrates. The activities of the two carboxymethylases were high in the rat brain in comparison to the other rat organs. The activity increased during the period of myelination in the rat brain. These findings suggest that carboxymethylation of myelin basic protein may play an important role in myelination.
在一项寻找羧甲基化天然底物蛋白的研究中,发现髓鞘碱性蛋白是一种良好的底物。以髓鞘碱性蛋白为底物,对两种蛋白质羧甲基化酶进行了部分纯化。这两种酶可能与已发现能使γ球蛋白甲基化的蛋白质羧甲基化酶I和II相同。与其他底物相比,髓鞘碱性蛋白的米氏常数(25微摩尔)非常小。与大鼠的其他器官相比,两种羧甲基化酶在大鼠脑中的活性较高。在大鼠脑髓鞘形成期间,该活性增加。这些发现表明,髓鞘碱性蛋白的羧甲基化可能在髓鞘形成中起重要作用。