人α -酪蛋白的磷酸化模式与反刍动物明显不同。

Esben S Sørensen, Lise Møller, Maria Vinther, Torben E Petersen, Lone K Rasmussen
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引用次数: 25

摘要

酪蛋白是高度磷酸化的牛奶蛋白,组装在称为胶束的大胶体结构中。在反刍动物的乳汁中,α - 1酪蛋白已被证明被广泛磷酸化。在本报告中,我们用基质辅助激光解吸质谱法和氨基酸序列分析相结合的方法确定了人α -酪蛋白的磷酸化模式。鉴定出三种磷酸化变异。一种非磷酸化的形式,一种变体在Ser18位点磷酸化,一种变体在Ser18和Ser26位点磷酸化。这两个磷酸化位点都位于乳腺酪蛋白激酶的氨基酸识别序列中。值得注意的是,在覆盖Ser70-Glu78残基的保守区域未观察到磷酸化,该区域在反刍动物α - 1酪蛋白中广泛磷酸化。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The phosphorylation pattern of human alphas1-casein is markedly different from the ruminant species.

Caseins are highly phosphorylated milk proteins assembled in large colloidal structures termed micelles. In the milk of ruminants, alphas1-casein has been shown to be extensively phosphorylated. In this report we have determined the phosphorylation pattern of human alphas1-casein by a combination of matrix-assisted laser desorption mass spectrometry and amino acid sequence analysis. Three phosphorylation variants were identified. A nonphosphorylated form, a variant phosphorylated at Ser18 and a variant phosphorylated at Ser18 and Ser26. Both phosphorylation sites are located in the amino acid recognition sequence of the mammary gland casein kinase. Notably, no phosphorylations were observed in the conserved region covering residues Ser70-Glu78, which is extensively phosphorylated in the ruminant alphas1-caseins.

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