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Structural characterization of glycopeptides by N-terminal protein ladder sequencing.
Anal Chem. 2006 Apr 01; 78(7):2239-43.AC

Abstract

High-sensitivity and high-throughput mass spectrometry (MS) has become an important tool for characterizing glycopeptides. Here, we analyzed synthetic O-linked glycopeptides using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) MS. First, we applied MALDI-quadrupole ion trap (QIT)-TOF MS, which enables collision-induced dissociation-MSn analysis for fine structural characterization. Subsequent MS/MS of sodium adduct ions selected as precursor ions yielded detailed information about the site of oligosaccharide attachment as well as the carbohydrate and amino acid sequences; however, these MS/MS spectra were very complex. To obtain easily interpretable and simple spectra, we used N-terminal protein ladder sequencing coupled with MALDI-TOF MS. From the extremely simple resulting spectra, we were able to determine the glycosylation sites, amino acid sequences, and oligosaccharide molecular weights of the glycopeptides.

Authors+Show Affiliations

Sphingolipid Expression Laboratory, Supra Biomolecular System Research Group, RIKEN Frontier Research System, Wako-shi, Saitama 351-0198, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16579603

Citation

Suzuki, Yusuke, et al. "Structural Characterization of Glycopeptides By N-terminal Protein Ladder Sequencing." Analytical Chemistry, vol. 78, no. 7, 2006, pp. 2239-43.
Suzuki Y, Suzuki M, Nakahara Y, et al. Structural characterization of glycopeptides by N-terminal protein ladder sequencing. Anal Chem. 2006;78(7):2239-43.
Suzuki, Y., Suzuki, M., Nakahara, Y., Ito, Y., Ito, E., Goto, N., Miseki, K., Iida, J., & Suzuki, A. (2006). Structural characterization of glycopeptides by N-terminal protein ladder sequencing. Analytical Chemistry, 78(7), 2239-43.
Suzuki Y, et al. Structural Characterization of Glycopeptides By N-terminal Protein Ladder Sequencing. Anal Chem. 2006 Apr 1;78(7):2239-43. PubMed PMID: 16579603.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural characterization of glycopeptides by N-terminal protein ladder sequencing. AU - Suzuki,Yusuke, AU - Suzuki,Minoru, AU - Nakahara,Yoshiaki, AU - Ito,Yukishige, AU - Ito,Emi, AU - Goto,Naoko, AU - Miseki,Kozo, AU - Iida,Junko, AU - Suzuki,Akemi, PY - 2006/4/4/pubmed PY - 2007/6/8/medline PY - 2006/4/4/entrez SP - 2239 EP - 43 JF - Analytical chemistry JO - Anal Chem VL - 78 IS - 7 N2 - High-sensitivity and high-throughput mass spectrometry (MS) has become an important tool for characterizing glycopeptides. Here, we analyzed synthetic O-linked glycopeptides using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) MS. First, we applied MALDI-quadrupole ion trap (QIT)-TOF MS, which enables collision-induced dissociation-MSn analysis for fine structural characterization. Subsequent MS/MS of sodium adduct ions selected as precursor ions yielded detailed information about the site of oligosaccharide attachment as well as the carbohydrate and amino acid sequences; however, these MS/MS spectra were very complex. To obtain easily interpretable and simple spectra, we used N-terminal protein ladder sequencing coupled with MALDI-TOF MS. From the extremely simple resulting spectra, we were able to determine the glycosylation sites, amino acid sequences, and oligosaccharide molecular weights of the glycopeptides. SN - 0003-2700 UR - https://www.unboundmedicine.com/medline/citation/16579603/Structural_characterization_of_glycopeptides_by_N_terminal_protein_ladder_sequencing_ L2 - https://doi.org/10.1021/ac051841x DB - PRIME DP - Unbound Medicine ER -