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<title>Mass spectrometry analysis of sulfated glycosaminoglycan oligosaccharides - Glycoscience Protocols (GlycoPODv2) - NCBI Bookshelf</title>
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<meta name="robots" content="INDEX,FOLLOW,NOARCHIVE" /><meta name="citation_inbook_title" content="Glycoscience Protocols (GlycoPODv2) [Internet]" /><meta name="citation_title" content="Mass spectrometry analysis of sulfated glycosaminoglycan oligosaccharides" /><meta name="citation_publisher" content="Japan Consortium for Glycobiology and Glycotechnology" /><meta name="citation_date" content="2022/03/15" /><meta name="citation_author" content="Shuhei Yamada" /><meta name="citation_pmid" content="37590650" /><meta name="citation_fulltext_html_url" content="https://www.ncbi.nlm.nih.gov/books/NBK593910/" /><meta name="citation_keywords" content="mass spectrometry (MS)" /><meta name="citation_keywords" content="sulfated oligosaccharide" /><meta name="citation_keywords" content="glycosaminoglycan" /><meta name="citation_keywords" content="heparan sulfate" /><meta name="citation_keywords" content="heparin" /><meta name="citation_keywords" content="chondroitin sulfate" /><link rel="schema.DC" href="http://purl.org/DC/elements/1.0/" /><meta name="DC.Title" content="Mass spectrometry analysis of sulfated glycosaminoglycan oligosaccharides" /><meta name="DC.Type" content="Text" /><meta name="DC.Publisher" content="Japan Consortium for Glycobiology and Glycotechnology" /><meta name="DC.Contributor" content="Shuhei Yamada" /><meta name="DC.Date" content="2022/03/15" /><meta name="DC.Identifier" content="https://www.ncbi.nlm.nih.gov/books/NBK593910/" /><meta name="description" content="Mass spectrometry (MS) is a great method to determine the mass of many biomaterials, including peptides, nucleotides, lipids, and oligosaccharides. Recent progresses in the analytical techniques of MS allow us to deduce structural details and quantify the amount of sulfated oligosaccharides derived from glycosaminoglycans (GAGs) (1,2). However, MS analysis of highly sulfated GAG oligosaccharides is still a severe task due to their poor mass spectrometric response and detrimental elimination of their sulfate groups during high energy ionization process. To improve this problem, the noncovalent complex formation with a basic peptide is extremely effective (3,4). The alkali cations, such as Na+ and K+, from the anionic groups of highly sulfated GAG oligosaccharides are completely displaced by basic polypeptides. 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To improve this problem, the noncovalent complex formation with a basic peptide is extremely effective (3,4). The alkali cations, such as Na+ and K+, from the anionic groups of highly sulfated GAG oligosaccharides are completely displaced by basic polypeptides. 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<div class="pre-content"><div><div class="bk_prnt"><p class="small">NCBI Bookshelf. A service of the National Library of Medicine, National Institutes of Health.</p><p>Nishihara S, Angata K, Aoki-Kinoshita KF, et al., editors. Glycoscience Protocols (GlycoPODv2) [Internet]. Saitama (JP): Japan Consortium for Glycobiology and Glycotechnology; 2021-. </p></div></div></div>
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<div class="main-content lit-style" itemscope="itemscope" itemtype="http://schema.org/CreativeWork"><div class="meta-content fm-sec"><h1 id="_NBK593910_"><span class="title" itemprop="name">Mass spectrometry analysis of sulfated glycosaminoglycan oligosaccharides</span></h1><div class="contrib half_rhythm"><span itemprop="author">Shuhei Yamada</span>, Ph.D.<div class="affiliation small">Meijo Univ.
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(Prof.)<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="pj.ca.u-ojiem@yiehuhs" class="oemail">pj.ca.u-ojiem@yiehuhs</a></div></div><div class="small">Corresponding author.</div></div><p class="small">Created: <span itemprop="datePublished">October 19, 2021</span>; Last Revision: <span itemprop="dateModified">March 15, 2022</span>.</p></div><div class="body-content whole_rhythm" itemprop="text"><div id="g147-sulfglycosamino.Introduction"><h2 id="_g147-sulfglycosamino_Introduction_">Introduction</h2><p>Mass spectrometry (MS) is a great method to determine the mass of many biomaterials, including peptides, nucleotides, lipids, and oligosaccharides. Recent progresses in the analytical techniques of MS allow us to deduce structural details and quantify the amount of sulfated oligosaccharides derived from glycosaminoglycans (GAGs) (<a class="bk_pop" href="#g147-sulfglycosamino.REF.1">1</a>,<a class="bk_pop" href="#g147-sulfglycosamino.REF.2">2</a>). However, MS analysis of highly sulfated GAG oligosaccharides is still a severe task due to their poor mass spectrometric response and detrimental elimination of their sulfate groups during high energy ionization process. To improve this problem, the noncovalent complex formation with a basic peptide is extremely effective (<a class="bk_pop" href="#g147-sulfglycosamino.REF.3">3</a>,<a class="bk_pop" href="#g147-sulfglycosamino.REF.4">4</a>). The alkali cations, such as Na<sup>+</sup> and K<sup>+</sup>, from the anionic groups of highly sulfated GAG oligosaccharides are completely displaced by basic polypeptides. MS signals of the highly sulfated GAG oligosaccharides are detected in the form of the ionic complex with a basic peptide, and their molecular weight can be determined by subtracting the molecular mass of the basic peptide from that of the complex.</p></div><div id="g147-sulfglycosamino.Protocol"><h2 id="_g147-sulfglycosamino_Protocol_">Protocol</h2><p>MS analysis of highly sulfated heparin oligosaccharides utilizing a noncovalent complex formation with a basic peptide.</p><div id="g147-sulfglycosamino.Materials"><h3>Materials</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Synthetic peptide Arg-(Gly-Arg)<sub>14</sub>-Gly (Peptide Institute, Inc., Osaka, Japan)</p></dd><dt>2.</dt><dd><p class="no_top_margin">2,5-dihydroxybenzoic acid (2,5-DHB) for Proteome Research (FUJIFILM Wako Pure Chemical Co., Osaka, Japan)</p></dd></dl></div><div id="g147-sulfglycosamino.Instrument"><h3>Instrument</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Matrix assisted laser desorption/ionization Time-of-flight (MALDI-TOF) MS (Voyager DE-RP/Pro, PerSeptive Biosystems, Framingham, MA)</p></dd></dl></div><div id="g147-sulfglycosamino.Methods"><h3>Methods</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Dissolve a sulfated oligosaccharide sample (10 pmol/μL) (<b>Note 1</b>).</p></dd><dt>2.</dt><dd><p class="no_top_margin">Prepare the matrix solution (10 mg/mL of 2,5-DHB in water) (<b>Note 2</b>).</p></dd><dt>3.</dt><dd><p class="no_top_margin">Prepare the peptide solution (10 pmol/μL) (<b>Note 3</b>).</p></dd><dt>4.</dt><dd><p class="no_top_margin">Add 1 μL of the peptide solution to the sample and vortex.</p></dd><dt>5.</dt><dd><p class="no_top_margin">Add 1 μL of the matrix solution to the mixture and vortex.</p></dd><dt>6.</dt><dd><p class="no_top_margin">Place an aliquot of the mixture on the probe surface and dry under a stream of air.</p></dd><dt>7.</dt><dd><p class="no_top_margin">Measure the sample by MALDI-TOF MS in the positive ion mode (<a class="figpopup" href="/books/NBK593910/figure/g147-sulfglycosamino.F1/?report=objectonly" target="object" rid-figpopup="figg147sulfglycosaminoF1" rid-ob="figobg147sulfglycosaminoF1">Figure 1</a>).</p></dd></dl></div><div id="g147-sulfglycosamino.Notes"><h3>Notes</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">In this protocol, a hexasulfated tetrasaccharide, 4-deoxy-α-L-<i>threo</i>-hex-4-enepyranosyluronic acid(2-<i>O</i>-sulfate)1-4-α-D-glucosamine(2-<i>N</i>-,6-<i>O</i>-disulfate)1-4-α-L-iduronic acid(2-<i>O</i>-sulfate)1-4-D-glucosamine(2-<i>N</i>-,6-<i>O</i>-disulfate) (<a class="figpopup" href="/books/NBK593910/figure/g147-sulfglycosamino.F1/?report=objectonly" target="object" rid-figpopup="figg147sulfglycosaminoF1" rid-ob="figobg147sulfglycosaminoF1">Figure 1</a>), prepared from heparin by digestion with heparinase and heparitinases was used as a representative (<a class="bk_pop" href="#g147-sulfglycosamino.REF.5">5</a>). Sulfated oligosaccharides from chondroitin sulfate are also available for this method (<a class="bk_pop" href="#g147-sulfglycosamino.REF.6">6</a>).</p></dd><dt>2.</dt><dd><p class="no_top_margin">This reagent should be prepared just before use.</p></dd><dt>3.</dt><dd><p class="no_top_margin">This solution can be stored at −80°C for a long period.</p></dd></dl></div></div><div id="g147-sulfglycosamino.References"><h2 id="_g147-sulfglycosamino_References_">References</h2><dl class="temp-labeled-list"><dt>1.</dt><dd><div class="bk_ref" id="g147-sulfglycosamino.REF.1">Zaia J. Glycosaminoglycan glycomics using mass spectrometry. <span><span class="ref-journal">Mol Cell Proteomics. </span>2013 Apr;<span class="ref-vol">12</span>(4):885–92.</span> [<a href="/pmc/articles/PMC3617335/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC3617335</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/23325770" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 23325770</span></a>] [<a href="http://dx.crossref.org/10.1074/mcp.R112.026294" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>2.</dt><dd><div class="bk_ref" id="g147-sulfglycosamino.REF.2">Turiák L, Tóth G, Ozohanics O, Révész Á, Ács A, Vékey K, Zaia J, Drahos L. Sensitive method for glycosaminoglycan analysis of tissue sections. <span><span class="ref-journal">J Chromatogr A. </span>2018 Apr 6;<span class="ref-vol">1544</span>:41–48.</span> [<a href="/pmc/articles/PMC6590710/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC6590710</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/29506752" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 29506752</span></a>] [<a href="http://dx.crossref.org/10.1016/j.chroma.2018.02.034" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>3.</dt><dd><div class="bk_ref" id="g147-sulfglycosamino.REF.3">Juhasz P, Biemann K. Utility of non-covalent complexes in the matrix-assisted laser desorption ionization mass spectrometry of heparin-derived oligosaccharides. <span><span class="ref-journal">Carbohydr Res. </span>1995 Apr 30;<span class="ref-vol">270</span>(2):131–47.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/7585697" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 7585697</span></a>] [<a href="http://dx.crossref.org/10.1016/0008-6215(94)00012-5" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>4.</dt><dd><div class="bk_ref" id="g147-sulfglycosamino.REF.4">Yamada S, Yamane Y, Tsuda H, Yoshida K, Sugahara K. A major common trisulfated hexasaccharide core sequence, hexuronic acid(2-sulfate)-glucosamine(<em>N</em>-sulfate)-iduronic acid-<em>N</em>-acetylglucosamine-glucuronic acid-glucosamine(<em>N</em>-sulfate), isolated from the low sulfated irregular region of porcine intestinal heparin. <span><span class="ref-journal">J Biol Chem. </span>1998 Mar 27;<span class="ref-vol">273</span>(13):7375–81.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/9442018" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 9442018</span></a>] [<a href="http://dx.crossref.org/10.1074/jbc.273.13.7375" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>5.</dt><dd><div class="bk_ref" id="g147-sulfglycosamino.REF.5">Yamada S, Sakamoto K, Tsuda H, Yoshida K, Sugahara K, Khoo KH, Morris HR, Dell A. Structural studies on the tri- and tetrasaccharides isolated from porcine intestinal heparin and characterization of heparinase/heparitinases using them as substrates. <span><span class="ref-journal">Glycobiology. </span>1994 Feb;<span class="ref-vol">4</span>(1):69–78.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/8186552" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 8186552</span></a>] [<a href="http://dx.crossref.org/10.1093/glycob/4.1.69" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>6.</dt><dd><div class="bk_ref" id="g147-sulfglycosamino.REF.6">Deepa SS, Yamada S, Fukui S, Sugahara K. Structural determination of novel sulfated octasaccharides isolated from chondroitin sulfate of shark cartilage and their application for characterizing monoclonal antibody epitopes. <span><span class="ref-journal">Glycobiology. </span>2007 Jun;<span class="ref-vol">17</span>(6):631–45.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/17317718" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17317718</span></a>] [<a href="http://dx.crossref.org/10.1093/glycob/cwm021" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd></dl></div><h2 id="NBK593910_footnotes">Footnotes</h2><dl class="temp-labeled-list small"><dt></dt><dd><div id="g147-sulfglycosamino.FN1"><p class="no_top_margin">The authors declare no competing or financial interests.</p></div></dd></dl><div class="bk_prnt_sctn"><h2>Figures</h2><div class="whole_rhythm bk_prnt_obj bk_first_prnt_obj"><div id="g147-sulfglycosamino.F1" class="figure bk_fig"><div class="graphic"><a href="/core/lw/2.0/html/tileshop_pmc/tileshop_pmc_inline.html?title=Figure%201%3A%20.%20Matrix%20assisted%20laser%20desorption%2Fionization%20Time-of-flight%20(MALDI-TOF)%20mass%20spectrum%20of%20the%20protonated%20complex%20of%20a%20hexasulfated%20tetrasaccharide.&p=BOOKS&id=593910_g147-sulfglycosamino-Image001.jpg" target="tileshopwindow" class="inline_block pmc_inline_block ts_canvas img_link" title="Click on image to zoom"><div class="ts_bar small" title="Click on image to zoom"></div><img src="/books/NBK593910/bin/g147-sulfglycosamino-Image001.jpg" alt="Figure 1: . Matrix assisted laser desorption/ionization Time-of-flight (MALDI-TOF) mass spectrum of the protonated complex of a hexasulfated tetrasaccharide." class="tileshop" title="Click on image to zoom" /></a></div><h3><span class="label">Figure 1: </span></h3><div class="caption"><p>Matrix assisted laser desorption/ionization Time-of-flight (MALDI-TOF) mass spectrum of the protonated complex of a hexasulfated tetrasaccharide. A heparin-derived hexasulfated tetrasaccharide was mixed with the basic peptide and delayed extraction MALDI-TOF mass spectrum of the protonated complex was recorded. The signals of the basic peptide and the noncovalent complex of the peptide and the saccharide were observed at <i>m/z</i> 3218.05 and 4369.27, respectively. Shown in parentheses is the mass of the saccharide after subtraction of the peptide mass. The structure and the graphical representation of the sulfated tetrasaccharide are shown above the spectrum (left and right, respectively). Pentagon, square, and diamond represents unsaturated hexuronic acid, glucosamine, and iduronic acid, respectively. 2S, 6S, and NS indicate 2-<i>O</i>-sulfate, 6-<i>O</i>-sulfate, and 2-<i>N</i>-sulfate, respectively.</p></div></div></div></div><div id="bk_toc_contnr"></div></div></div>
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<div class="post-content"><div><div class="half_rhythm"><a href="/books/about/copyright/">Copyright Notice</a><p class="small">Licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 Unported license. To view a copy of this license, visit <a href="http://creativecommons.org/licenses/by-nc-nd/4.0/" ref="pagearea=meta&targetsite=external&targetcat=link&targettype=uri">http://creativecommons.org/licenses/by-nc-nd/4.0/</a>.</p></div><div class="small"><span class="label">Bookshelf ID: NBK593910</span><span class="label">PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/37590650" title="PubMed record of this page" ref="pagearea=meta&targetsite=entrez&targetcat=link&targettype=pubmed">37590650</a></span></div><div style="margin-top:2em" class="bk_noprnt"><a class="bk_cntns" href="/books/n/glycopodv2/">Contents</a><div class="pagination bk_noprnt"><a class="active page_link prev" href="/books/n/glycopodv2/g146-glycosaminsites/" title="Previous page in this title">< Prev</a><a class="active page_link next" href="/books/n/glycopodv2/nuclear/" title="Next page in this title">Next ></a></div></div></div></div>
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