Electrospray ionization Fourier transform mass spectrometric analysis of intact bikunin glycosaminoglycan from normal human plasma

Tatiana N. Laremore, Franklin E. Leach, I. Jonathan Amster, Robert J. Linhardt

6 Scopus citations

Abstract

A mixture of glycosaminoglycan (GAG) chains from a plasma proteoglycan bikunin was fractionated using native, continuous-elution polyacrylamide gel electrophoresis, and the resulting fractions were analyzed by electrospray ionization Fourier transform mass spectrometry (ESI FTMS). Molecular mass analysis of the intact GAG afforded information about the length and composition of GAG chains in the mixture. Ambiguity in the interpretation of the intact GAG mass spectra was eliminated by conducting an additional experiment in which the GAG chains of known molecular mass were treated with a GAG-degrading enzyme, chondroitinase ABC, and the digestion products were analyzed by ESI FTMS. The plasma bikunin GAG chains consisted predominantly of odd number of saccharides, although few chains consisting of even number of saccharides were also detected. Majority of the analyzed chains were tetrasulfated or pentasulfated and comprised by 29-41 monosaccharides.

Original languageEnglish (US)
Pages (from-to)109-115
Number of pages7
JournalInternational Journal of Mass Spectrometry
Volume305
Issue number2-3
DOIs
Publication statusPublished - Aug 15 2011

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All Science Journal Classification (ASJC) codes

  • Instrumentation
  • Condensed Matter Physics
  • Spectroscopy
  • Physical and Theoretical Chemistry

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