磷酸化
磷蛋白
牛乳
磷酸蛋白质组学
小桶
婴儿配方奶粉
生物
哺乳期
蛋白质磷酸化
蛋白质组学
生物化学
计算生物学
基因本体论
基因
遗传学
蛋白激酶A
基因表达
怀孕
作者
Binsong Han,Lina Zhang,Ying Ma,Yanmei Hou,Kui Xie,Jinjing Zhong,Peng Zhou
标识
DOI:10.1021/acs.jafc.2c07326
摘要
Phosphorylation is a broad post-translational protein modification, and the level of phosphorylation of milk proteins is associated with lactation, coagulation properties, and digestibility. However, phosphoproteins in bovine milk-based and goat milk-based infant formula have not been systematically explored. Here, we have analyzed six bovine and six goat milk-based infant formula using a quantitative phosphoproteomics approach, from which we identified 200 phosphoproteins with 276 phosphorylation sites and 156 phosphorylation sites from 75 phosphoproteins, respectively. Of these, 99 phosphorylation sites from 26 shared phosphoproteins were differentially expressed between bovine and goat milk-based infant formula. Especially, CSN1S1 was the most phosphoprotein with 25 quantified phosphorylation sites. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analyses showed that the identified phosphoproteins not only provide nutrition to the infant but also have anti-inflammatory, antipathogenic, and other biological functions. Our results shed light on the composition, phosphorylation sites, and biological functions of phosphoproteins in bovine milk and goat milk-based infant formula, which provide new insights into the key role of protein modifications during infant development. It also helps us to better understand the differences in digestibility of infant formula from different animal milk sources and thus guides the choice of milk source for infant formula.
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