Analysis of Peptide
Mapping，Glycosylated
Site and Glycan Structure in Ribonuclease B by Liquid
Chromatography-Electrospray Mass Spectrometry
ZENG Rong，SHAO Xiao-Xia，WANG ke-Yi and XIA Qi-Chang
( Shanghai Institute of Biochemistry， Chinese Academy of Sciences， Shanghai 200031， China )
Abstract Liquid
chromatography-electrospray mass spectrometry was utilized to analyze peptide
mapping of aglycoprotein，ribonuclease B，to obtain its primary structure.The
glycosylated site was determined by comparison of peptide mapping before and
after glycanase treatment.Tandem MS(MS/MS)was performed to analyze the
structure of N-linked glycan and deglycosylated peptide.The nature of glycan
was determined to be of highmannose type by mass spectrometry after the
treatment with α-mannosidase.In addition，the relative abundance of
heterogeneous glycopeptides was quantified.This method is rapid and sensitive
for the characterization of glycoproteins with N-linked glycan.
Key Words liquid chromatography-electrospray
mass spectrometry；glycoprotein；glycosylated site；glycoform；ribonulease B
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