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

Authors
Laremore, Tatiana N.
Leach, Franklin E.
Amster, I. Jonathan
Linhardt, Robert J.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2011-08-15
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
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Full Citation
Electrospray ionization Fourier transform mass spectrometric analysis of intact bikunin glycosaminoglycan from normal human plasma, T. N. Laremore, F. E. Leach III, I. J. Amster, R. J. Linhardt, International Journal of Mass Spectrometry, 305, 109–115, 2011.
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.
Description
International Journal of Mass Spectrometry, 305, 109–115
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
International Journal of Mass Spectrometry
https://harc.rpi.edu/
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