Sequence and N-glycan diversity analysis of immunoglobulin G from buffalo milk using RP-UHPLC MS/MS
| Autor: | B. S. Gnanesh Kumar, P. Lijina, P. Jinesh |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Glycan 030102 biochemistry & molecular biology biology Sequence analysis Chemistry Organic Chemistry Clinical Biochemistry food and beverages Immunoglobulin light chain Biochemistry Immunoglobulin G 03 medical and health sciences 030104 developmental biology N-linked glycosylation biology.protein Colostrum Peptide sequence Fucosylation |
| Zdroj: | Amino Acids. 53:533-539 |
| ISSN: | 1438-2199 0939-4451 |
| DOI: | 10.1007/s00726-021-02945-5 |
| Popis: | Immunoglobulin G is the abundant antibody present in the colostrum and milk of major dairy animals. In the present study, buffalo milk IgG was characterized for its amino acid sequence and glycan diversity using reverse phase liquid chromatography coupled to ESI-Q-TOF MS in tandem mode. Amino acid sequence analysis of heavy chain constant region revealed the presence of two IgG subtypes namely IgG1 and IgG3, with IgG1 being the abundant. The complete light chain constant region sequence was also determined. N-glycan sequence analysis at a highly conserved site Asn-Ser-Thr revealed the presence of mainly biantennary complex type with core fucosylation (34%), bisecting GlcNAc (19%) and sialylation with both Neu5Ac and Neu5Gc (14%). The observed glycan diversity in buffalo milk IgG is in part comparable with bovine colostrum as well as human, bovine, goat serum counterparts. |
| Databáze: | OpenAIRE |
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