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Food Chem ; 419: 136081, 2023 Sep 01.
Article in English | MEDLINE | ID: mdl-37037133

ABSTRACT

Milk fat globule membrane (MFGM) proteins are highly glycosylated and involved in various biological processes within the body. However, information on site-specific N-glycosylation of MFGM glycoproteins in donkey and human milk remains limited. This study aimed to map the most comprehensive site-specific N-glycosylation fingerprinting of donkey and human MFGM glycoproteins using a site-specific glycoproteomics strategy. We identified 1,360, 457, 2,617, and 986 site-specific N-glycans from 296, 77, 214, and 196 N-glycoproteins in donkey colostrum (DC), donkey mature milk (DM), human colostrum (HC), and human mature milk (HM), respectively. Bioinformatics was used to describe the structure-activity relationships of DC, DM, HC, and HM MFGM N-glycoproteins. The results revealed differences in the molecular composition of donkey and human MFGM N-glycoproteins and the dynamic changes to site-specific N-glycosylation of donkey and human MFGM glycoproteins during lactation, deepening our understanding of the composition of donkey and human MFGM N-glycoproteins and their potential physiological roles.


Subject(s)
Colostrum , Proteome , Animals , Female , Humans , Pregnancy , Colostrum/metabolism , Equidae , Glycolipids , Glycoproteins/metabolism , Glycosylation , Lipid Droplets/metabolism , Milk Proteins/metabolism , Milk, Human/metabolism , Proteome/metabolism , Proteomics , Tandem Mass Spectrometry
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