Abstract

Timetable

Download Conference Program

Download All Abstracts

Zoom Access

Plenary Lectures Day1　Day2　Day3　Day4

MSSJ Award Lectures Day1

Oral Sessions Day2　Day3　Day4

Poster Presentations Day1　Day2　Day3　Day4

Late-Breaking Posters Day1

Luncheon Seminars Day2　Day3　Day4

Teatime Sessions Day3

Corporate Posters Day2　Day3　Day4

Corporate Program

Poster Presentations

Day 4, June 25（Wed.）　

Room P (Maesato East, Foyer, Ocean Wing)

• 4P-AM-14
• PDF

Derivatization methods of sialylated glycans using lactone ring-opening aminolysis and lactone-driven ester-to-amide conversion for MALDI-TOF MS analysis

(¹Nagoya Univ., ²Hokkaido Univ., ³Shimadzu corp.)
^oJun-ichi Furukawa^1,2, Takashi Nishikaze³, Masaki Kurogochi¹, Hisatoshi Hanamatsu¹

Glycosylation is one of the most important posttranslational modifications of proteins and plays crucial roles in numerous biological processes. A portion of Lipids are also glycosylated, and glycosphingolipids are a major sub-class of glycolipids. Sialic acid is a representative acidic monosaccharide residue and N-acetylneuraminic acid is the predominant sialic acid form in human. Sialic acid is the terminal sugar in N-, GSL-, and O-glycans attached via α2,3- and α2,6-linkages, resulting to form structural isomers. Glycan isomers with different sialic acid linkage cannot be distinguished by MS analysis due to the same molecular weight.
In the present study, we report two different procedures of sialic acid linkage-specific alkylamidation by intramolecular lactone ring-opening aminolysis and lactone-driven ester-to-amide derivatization.

---