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- W4296200825 abstract "Donkey colostrum milk fat globule membrane (DCMFGM) proteins are involved in multiple biological functions. However, the effect of N-glycosylation on their physiological properties are unknown. The aim of this study was to map the DCMFGM protein site-specific N-glycosylation landscape using a label-free glycoproteomic approach. A total of 1,443 unique intact N-glycopeptides mapping to 453 unique N-glycosites on 336 N-glycoproteins were identified. The macro- and microheterogeneity of DCMFGM glycoproteins were explored at the N-glycosite level and the site-specific N-glycan level, respectively, and it was found that the N-glycosylation profiles of the DCMFGM proteins varied based on subcellular localisation and protein domain types. Our findings reveal the heterogeneity and functional diversity of N-glycosylation of DCMFGM proteins and provide theoretical support for the promotion of DCMFGM proteins as a functional food ingredient." @default.
- W4296200825 created "2022-09-18" @default.
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- W4296200825 date "2022-12-01" @default.
- W4296200825 modified "2023-09-27" @default.
- W4296200825 title "A new sight to explore site-specific N-glycosylation in donkey colostrum milk fat globule membrane proteins with glycoproteomics analysis." @default.
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- W4296200825 doi "https://doi.org/10.1016/j.foodres.2022.111938" @default.
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