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首页> 外文期刊>Biochemistry >Determination of the sites of posttranslational modifications in the charge isomers of bovine myelin basic protein by capillary electrophoresis mass spectroscopy
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Determination of the sites of posttranslational modifications in the charge isomers of bovine myelin basic protein by capillary electrophoresis mass spectroscopy

机译：毛细管电泳质谱法测定牛髓磷脂碱性蛋白的电荷异构体中翻译后修饰的位点

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摘要

The posttranslational modifications in each of the 18.5 kDa bovine myelin basic protein charge isomers C-1 to C-6 have been determined by the use of capillary electrophoresis-mass spectroscopy. The pattern of modifications is viewed as being unique to each charge isomer and is thought to reflect a specific placement and function for each isomer in the myelin membrane. Several of the sites of posttranslational phosphorylation were found to differ from a number of the reported sites that were phosphorylated in vitro by various kinases. These differences suggest that an extremely cautious approach be taken in identifying in vivo posttranslationally modified amino acid residues from residues that have been modified in vitro by various kinases. We have identified the following posttranslationally phosphorylated and deamidated, modified sites in the bovine MBP components C1-C6. C1 has no modification; C2 represents a deamidation of Gin 146; in C3, Thr 97 and Ser 164 are phosphorylated; in C4, Ser 54, Thr 97, and Ser 160 are phosphorylated; in C5 Ser 7, Ser 54, Thr 97, and Ser 164 are phosphorylated; anti in C6, Ser 7, Ser 54, Thr 97, Ser 160, and Ser 164 are phosphorylated. [References: 43]
机译：已通过使用毛细管电泳-质谱法确定了每个18.5 kDa的牛髓磷脂碱性蛋白电荷异构体C-1至C-6的翻译后修饰。修饰的模式被认为是每种电荷异构体所独有的，并且被认为反映了髓磷脂膜中每种异构体的特定位置和功能。发现翻译后磷酸化的几个位点与许多报道的在体外被各种激酶磷酸化的位点不同。这些差异表明，在从体内已被各种激酶修饰的残基中鉴定出体内翻译后修饰的氨基酸残基时，应采取极为谨慎的方法。我们在牛MBP组分C1-C6中鉴定了以下翻译后磷酸化和脱酰胺基修饰的位点。 C1没有修改; C2代表杜松子糖146的脱酰胺基;在C3中，Thr 97和Ser 164被磷酸化;在C4中，Ser 54，Thr 97和Ser 160被磷酸化;在C5中，Ser 7，Ser 54，Thr 97和Ser 164被磷酸化; C6中的抗，Ser 7，Ser 54，Thr 97，Ser 160和Ser 164磷酸化。 [参考：43]

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