Analysis of N-linked Oligosaccharides from Xenopus laevis Vitelline Envelope Glycoprotein ZPA by Mass Spectrometry

Document Type

Conference Presentation

Department

Chemistry

Conference Title

239th American Chemical Society (ACS) National Meeting

Organization

American Chemical Society (ACS)

Location

San Francisco, CA

Conference Dates

March 21-25, 2010

Date of Presentation

3-23-2010

Abstract

Glycoprotein ZPA, is the least abundant component of the four vitelline envelop glycoproteins (ZPA, ZPB, ZPC and ZPX) of Xenopus laevis egg. Oligosaccharides from these types of glycoproteins are believed to play key roles in fertilization process, which may include protection of eggs against pathogens, initiation of sperm capacitation or the acrosome reaction, species-specific interaction of gametes, and prevention of polyspermy. Knowledge of the glycosylation of ZPA is rudimentary and no structural details for the glycans are known. Here we report progress towards the structure elucidation of N-linked glycans from ZPA. After SDS-PAGE separation, ZPA was firstly in-gel digested followed by enrichment through lectin affinity and/or liquid chromatography. Glycans were released from the glycopeptides through PNGaseF. Both glycopeptides and glycans were characterized by mass spectrometry.

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