nih-gov/www.ncbi.nlm.nih.gov/books/NBK593973/index.html?report=printable

108 lines
No EOL
29 KiB
XML
Raw Blame History

This file contains ambiguous Unicode characters

This file contains Unicode characters that might be confused with other characters. If you think that this is intentional, you can safely ignore this warning. Use the Escape button to reveal them.

<?xml version="1.0" encoding="utf-8"?>
<!DOCTYPE html PUBLIC "-//W3C//DTD XHTML 1.0 Transitional//EN" "http://www.w3.org/TR/xhtml1/DTD/xhtml1-transitional.dtd">
<html xmlns="http://www.w3.org/1999/xhtml" xml:lang="en" lang="en">
<head><meta http-equiv="Content-Type" content="text/html; charset=utf-8" />
<!-- AppResources meta begin -->
<meta name="paf-app-resources" content="" />
<script type="text/javascript">var ncbi_startTime = new Date();</script>
<!-- AppResources meta end -->
<!-- TemplateResources meta begin -->
<meta name="paf_template" content="" />
<!-- TemplateResources meta end -->
<!-- Logger begin -->
<meta name="ncbi_db" content="books" /><meta name="ncbi_pdid" content="book-part" /><meta name="ncbi_acc" content="NBK593973" /><meta name="ncbi_domain" content="glycopodv2" /><meta name="ncbi_report" content="printable" /><meta name="ncbi_type" content="fulltext" /><meta name="ncbi_objectid" content="" /><meta name="ncbi_pcid" content="/NBK593973/?report=printable" /><meta name="ncbi_app" content="bookshelf" />
<!-- Logger end -->
<title>Purification method for serum free glycans - Glycoscience Protocols (GlycoPODv2) - NCBI Bookshelf</title>
<!-- AppResources external_resources begin -->
<link rel="stylesheet" href="/core/jig/1.15.2/css/jig.min.css" /><script type="text/javascript" src="/core/jig/1.15.2/js/jig.min.js"></script>
<!-- AppResources external_resources end -->
<!-- Page meta begin -->
<meta name="robots" content="INDEX,FOLLOW,NOARCHIVE" /><meta name="citation_inbook_title" content="Glycoscience Protocols (GlycoPODv2) [Internet]" /><meta name="citation_title" content="Purification method for serum free glycans" /><meta name="citation_publisher" content="Japan Consortium for Glycobiology and Glycotechnology" /><meta name="citation_date" content="2022/03/24" /><meta name="citation_author" content="Chengcheng Huang" /><meta name="citation_author" content="Tadashi Suzuki" /><meta name="citation_pmid" content="37590704" /><meta name="citation_fulltext_html_url" content="https://www.ncbi.nlm.nih.gov/books/NBK593973/" /><meta name="citation_keywords" content="serum" /><meta name="citation_keywords" content="sialyl free N-glycans (sialyl FNGs)" /><meta name="citation_keywords" content="neutral free N-glycans (neutral FNGs)" /><meta name="citation_keywords" content="small-sialyl glycans" /><link rel="schema.DC" href="http://purl.org/DC/elements/1.0/" /><meta name="DC.Title" content="Purification method for serum free glycans" /><meta name="DC.Type" content="Text" /><meta name="DC.Publisher" content="Japan Consortium for Glycobiology and Glycotechnology" /><meta name="DC.Contributor" content="Chengcheng Huang" /><meta name="DC.Contributor" content="Tadashi Suzuki" /><meta name="DC.Date" content="2022/03/24" /><meta name="DC.Identifier" content="https://www.ncbi.nlm.nih.gov/books/NBK593973/" /><meta name="description" content="Recent studies have indicated the occurrence of sialyl free N-glycans (FNGs) in sera (1,2). These glycans have been purified from the serum using a 3K-amicon followed by a PD-10 column and 2-aminopyridine (PA)-labeling for detecting glycans in the previous study. We optimized the glycan purification method, and using this method, we could identify glycans that were missed when using the previous amicon-purification method. Here we will introduce our optimized glycan purification method (3)." /><meta name="og:title" content="Purification method for serum free glycans" /><meta name="og:type" content="book" /><meta name="og:description" content="Recent studies have indicated the occurrence of sialyl free N-glycans (FNGs) in sera (1,2). These glycans have been purified from the serum using a 3K-amicon followed by a PD-10 column and 2-aminopyridine (PA)-labeling for detecting glycans in the previous study. We optimized the glycan purification method, and using this method, we could identify glycans that were missed when using the previous amicon-purification method. Here we will introduce our optimized glycan purification method (3)." /><meta name="og:url" content="https://www.ncbi.nlm.nih.gov/books/NBK593973/" /><meta name="og:site_name" content="NCBI Bookshelf" /><meta name="og:image" content="https://www.ncbi.nlm.nih.gov/corehtml/pmc/pmcgifs/bookshelf/thumbs/th-glycopodv2-lrg.png" /><meta name="twitter:card" content="summary" /><meta name="twitter:site" content="@ncbibooks" /><meta name="bk-non-canon-loc" content="/books/n/glycopodv2/g19-methodglycans/" /><link rel="canonical" href="https://www.ncbi.nlm.nih.gov/books/NBK593973/" /><link rel="stylesheet" href="/corehtml/pmc/css/figpopup.css" type="text/css" media="screen" /><link rel="stylesheet" href="/corehtml/pmc/css/bookshelf/2.26/css/books.min.css" type="text/css" /><link rel="stylesheet" href="/corehtml/pmc/css/bookshelf/2.26/css/books_print.min.css" type="text/css" /><style type="text/css">p a.figpopup{display:inline !important} .bk_tt {font-family: monospace} .first-line-outdent .bk_ref {display: inline} </style><script type="text/javascript" src="/corehtml/pmc/js/jquery.hoverIntent.min.js"> </script><script type="text/javascript" src="/corehtml/pmc/js/common.min.js?_=3.18"> </script><script type="text/javascript">window.name="mainwindow";</script><script type="text/javascript" src="/corehtml/pmc/js/bookshelf/2.26/book-toc.min.js"> </script><script type="text/javascript" src="/corehtml/pmc/js/bookshelf/2.26/books.min.js"> </script>
<!-- Page meta end -->
<link rel="shortcut icon" href="//www.ncbi.nlm.nih.gov/favicon.ico" /><meta name="ncbi_phid" content="CE8E40FC7D674B510000000000080007.m_5" />
<meta name='referrer' content='origin-when-cross-origin'/><link type="text/css" rel="stylesheet" href="//static.pubmed.gov/portal/portal3rc.fcgi/4216699/css/3852956/3985586/3808861/4121862/3974050/3917732/251717/4216701/14534/45193/4113719/3849091/3984811/3751656/4033350/3840896/3577051/3852958/3984801/12930/3964959.css" /><link type="text/css" rel="stylesheet" href="//static.pubmed.gov/portal/portal3rc.fcgi/4216699/css/3411343/3882866.css" media="print" /></head>
<body class="book-part">
<div class="grid no_max_width">
<div class="col twelve_col nomargin shadow">
<!-- System messages like service outage or JS required; this is handled by the TemplateResources portlet -->
<div class="sysmessages">
<noscript>
<p class="nojs">
<strong>Warning:</strong>
The NCBI web site requires JavaScript to function.
<a href="/guide/browsers/#enablejs" title="Learn how to enable JavaScript" target="_blank">more...</a>
</p>
</noscript>
</div>
<!--/.sysmessage-->
<div class="wrap">
<div class="page">
<div class="top">
<div class="header">
</div>
<!--<component id="Page" label="headcontent"/>-->
</div>
<div class="content">
<!-- site messages -->
<div class="container content">
<div class="document">
<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>
<div class="main-content lit-style" itemscope="itemscope" itemtype="http://schema.org/CreativeWork"><div class="meta-content fm-sec"><h1 id="_NBK593973_"><span class="title" itemprop="name">Purification method for serum free glycans</span></h1><div class="contrib half_rhythm"><span itemprop="author">Chengcheng Huang</span>, Ph.D<div class="affiliation small">Glycometabolic Biochemistry Laboratory, RIKEN CPR<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="pj.nekir@gcgcgh" class="oemail">pj.nekir@gcgcgh</a></div></div><div class="small">Corresponding author.</div></div><div class="contrib half_rhythm"><span itemprop="author">Tadashi Suzuki</span>, Ph.D<div class="affiliation small">Glycometabolic Biochemistry Laboratory, RIKEN CPR<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="pj.nekir@mg_ikuzust" class="oemail">pj.nekir@mg_ikuzust</a></div></div></div><p class="small">Created: <span itemprop="datePublished">November 2, 2021</span>; Last Revision: <span itemprop="dateModified">March 24, 2022</span>.</p></div><div class="body-content whole_rhythm" itemprop="text"><div id="g19-methodglycans.Introduction"><h2 id="_g19-methodglycans_Introduction_">Introduction</h2><p>Recent studies have indicated the occurrence of sialyl free <i>N</i>-glycans (FNGs) in sera (<a class="bk_pop" href="#g19-methodglycans.REF.1">1</a>,<a class="bk_pop" href="#g19-methodglycans.REF.2">2</a>). These glycans have been purified from the serum using a 3K-amicon followed by a PD-10 column and 2-aminopyridine (PA)-labeling for detecting glycans in the previous study. We optimized the glycan purification method, and using this method, we could identify glycans that were missed when using the previous amicon-purification method. Here we will introduce our optimized glycan purification method (<a class="bk_pop" href="#g19-methodglycans.REF.3">3</a>).</p></div><div id="g19-methodglycans.Protocol"><h2 id="_g19-methodglycans_Protocol_">Protocol</h2><p>This protocol first eliminates the serum proteins using ethanol precipitation, and the remaining water-soluble fractions are purified by a graphite carbon (GC) column followed by a PD-10 column, and the purified glycans are then labeled with PA for high-performance liquid chromatography (HPLC) analysis. Here the GC column is used instead of a 3K-amicon before the PD-10 purification in the previous method that was used for serum analysis (<a class="bk_pop" href="#g19-methodglycans.REF.2">2</a>).</p><div id="g19-methodglycans.Materials"><h3>Materials</h3><p>1. Ethanol (HPLC level)</p><p>2. InsertSepGC column (150 mg/3 mL, GL science, Tokyo, Japan)</p><p>3. PD-10 column (GE Healthcare, Chicago, IL)</p><p>4. 2-Aminopyridine (PA) (3 g/mL in acetic acid) (Note 1)</p><p>5. Di-methylamine-borane (0.5 mg/mL in acetic acid) (Note 2)</p><p>6. MonoFas column (GL science)</p><p>7. Elution solution: 50% acetonitrile, with 20 mM of triethylamine-acetic acid (AcOH) pH 6.0 (Note 3).</p><p>8. 5% Ethanol</p><p>9. Acetonitrile (ACN), 100% and 95%.</p><p>10. TSKgel diethylaminoethanol (DEAE)-5PW column (7.5 &#x003d5; &#x000d7; 75 mm; Tosoh, Tokyo, Japan)</p><p>11. Shodex NH2P-40-3E column (3.0 mm &#x003d5; &#x000d7; 250 mm, Shodex, Tokyo, Japan)</p><p>12. Inertsil ODS-3 column (2.1 &#x003d5; &#x000d7; 150 mm; GL Sciences)</p><p>13. DEAE anion exchange A buffer: 10% acetonitrile containing 0.01% triethylamine.</p><p>14. DEAE anion exchange B buffer: 10% acetonitrile, with 7.4% triethylamine and 3% acetic acid.</p><p>15. Size fractionation A buffer: 93% acetonitrile in 0.3% acetate buffer (pH 7.0 adjusted by ammonia).</p><p>16. Size fractionation B buffer: 20% acetonitrile in 0.3% acetate buffer (pH 7.0 adjusted by ammonia).</p><p>17. Dual-gradient reversed-phase A buffer: 0.1 M ammonium acetate buffer, pH 6.4.</p><p>18. Dual-gradient reversed-phase B buffer: 0.1 M ammonium acetate buffer, pH 4.0 with 0.5% 1-butanol.</p><p>19. Jack bean mannosidase (JB man&#x02019;ase) (Seikagaku Biobusiness Corporation, Japan).</p><p>20. Sialidase (Arthrobacter ureafaciens) (Roche Applied Science, Penzberg, Germany)</p><p>21. 10&#x000d7; Sialidase/JB man&#x02019;ase reaction buffer: 500 mM of sodium citrate buffer, pH 4.5.</p></div><div id="g19-methodglycans.Instruments"><h3>Instruments</h3><p>1. GL science HPLC system (PUC double pumps/CO630 column oven) with a fluorescence detector (LaChrome, HITACHI High technologies, Tokyo, Japan) or equivalent.</p><p>2. pH meter</p><p>3. Vacuum evaporator</p><p>4. High-speed refrigerated centrifuge</p></div><div id="g19-methodglycans.Methods"><h3>Methods</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Pretreatment of serum</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Add 1.5 volume of ethanol to the serum, mix, and incubate on ice for 10 min (<b>Note 4</b>).</p></dd><dt>b.</dt><dd><p class="no_top_margin">Centrifuge at 17,000 &#x000d7;<i>g</i> for 10 min at 4&#x000b0;C.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Take the supernatant and transfer to the new tube; dry the supernatant using a vacuum evaporator.</p></dd><dt>d.</dt><dd><p class="no_top_margin">Dissolve the sample in 0.5&#x02013;1 mL of dH<sub>2</sub>O.</p></dd></dl></dd><dt>2.</dt><dd><p class="no_top_margin">Sample desalting by GC column</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Prepare the GC column pretreated with 2 mL of 100% ACN.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Wash the column twice with 5 mL of dH<sub>2</sub>O.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Load sample on the GC column and discard the flowthrough.</p></dd><dt>d.</dt><dd><p class="no_top_margin">Wash column twice with 5 mL of dH<sub>2</sub>O.</p></dd><dt>e.</dt><dd><p class="no_top_margin">Elute the sample with 2.5 mL of elution solution, and collect the sample in a 15-mL tube.</p></dd><dt>f.</dt><dd><p class="no_top_margin">Dry the eluate using a vacuum evaporator (<b>Note 5</b>).</p></dd><dt>g.</dt><dd><p class="no_top_margin">Dissolve the sample with 0.5 mL of dH<sub>2</sub>O for a PD-10 desalting.</p></dd></dl></dd><dt>3.</dt><dd><p class="no_top_margin">A second-step desalting by PD-10</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Wash the PD-10 desalting column with 25 mL of 5% ethanol.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Load 0.5 mL of sample from Step 2g on the column.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Load 2 mL of 5% ethanol; discard the eluate.</p></dd><dt>d.</dt><dd><p class="no_top_margin">Add 3.5 mL of 5% ethanol and collect the eluate in a new 15-mL Falcon tube.</p></dd><dt>e.</dt><dd><p class="no_top_margin">Dry the eluate using a vacuum evaporator.</p></dd></dl></dd><dt>4.</dt><dd><p class="no_top_margin">PA-labeling</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Using the dried sample from Step 3e, redissolve the sample in 30 &#x003bc;L of dH<sub>2</sub>O, and dry up the sample by a vacuum evaporator (<b>Note 6</b>).</p></dd><dt>b.</dt><dd><p class="no_top_margin">Dissolve the sample with 20 &#x003bc;L of PA in AcOH. Incubate the sample at 80&#x000b0;C for 90 min.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Add 20 &#x003bc;L of di-methylamine-borane in AcOH to the sample. Incubate at 80&#x000b0;C for another 60 min.</p></dd><dt>d.</dt><dd><p class="no_top_margin">Wash a clean MonoFas spin column with 200 &#x003bc;L of dH<sub>2</sub>O, followed by 800 &#x003bc;L 100% ACN, and discard the eluate.</p></dd><dt>e.</dt><dd><p class="no_top_margin">Add 460 &#x003bc;L of acetonitrile to the PA-labeled sample, mix, and load on the pretreated MonoFas spin column.</p></dd><dt>f.</dt><dd><p class="no_top_margin">Centrifuge for 10,000 &#x000d7;<i>g</i> for 1 min.</p></dd><dt>g.</dt><dd><p class="no_top_margin">Wash the MonoFas spin column with 500 &#x003bc;L of 95% ACN, apply the solution on the MonoFas spin column, centrifuge for 10,000 &#x000d7;<i>g</i> for 1 min, and discard the flowthrough.</p></dd><dt>h.</dt><dd><p class="no_top_margin">Wash the MonoFas spin column with 800 &#x003bc;L of 95% ACN and discard the flowthrough.</p></dd><dt>i.</dt><dd><p class="no_top_margin">Set the spin column to a clean 1.5-mL collection tube, add 200 &#x003bc;L of dH<sub>2</sub>O on the column, and collect the eluate after centrifugation at 10,000 &#x000d7;<i>g</i> for 1 min.</p></dd></dl></dd><dt>5.</dt><dd><p class="no_top_margin">Detection of glycans by HPLC (<a class="bk_pop" href="#g19-methodglycans.REF.4">4</a>)</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Treat sample with sialidase to identify sialylated free glycans.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Apply the sample to DEAE anion exchange HPLC (DEAE-5PW column) (<a class="bk_pop" href="#g19-methodglycans.REF.3">3</a>).</p></dd><dt>c.</dt><dd><p class="no_top_margin">HPLC elution conditions and detection of the PA-labeled glycans are as follows:</p><p>Gradient program (% of DEAE anion exchange B buffer, 1 mL/min, at 25&#x000b0;C):</p><p>0&#x02013;5 min, isocratic 0%;</p><p>5&#x02013;45 min, 0%&#x02013;20%;</p><p>45&#x02013;50 min, isocratic 100%;</p><p>50&#x02013;60 min, isocratic 0%.</p><p>Emission wavelength: 380 nm and Excitation wavelength: 310 nm.</p></dd><dt>d.</dt><dd><p class="no_top_margin">For sialyl free glycans, collect sialidase-sensitive peaks for further analysis (<a class="figpopup" href="/books/NBK593973/figure/g19-methodglycans.F1/?report=objectonly" target="object" rid-figpopup="figg19methodglycansF1" rid-ob="figobg19methodglycansF1">Figure 1</a>) (<b>Note 7</b>).</p></dd><dt>e.</dt><dd><p class="no_top_margin">For the analysis of neutral glycans, collect the flowthrough fraction of the DEAE HPLC and apply to a size fractionation HPLC (NH2P-40-3E column) with the following elution conditions (% of size fractionation B buffer, 0.45 mL/min at 25&#x000b0;C):</p><p>0&#x02013;0.5 min, 1%&#x02013;10%;</p><p>0.5&#x02013;3 min, 10%&#x02013;25%;</p><p>3&#x02013;33 min, 25%&#x02013;55%;</p><p>33.1&#x02013;35 min, isocratic 70%;</p><p>35.1&#x02013;55 min, isocratic 1%.</p><p>Emission wavelength: 380 nm and Excitation wavelength: 310 nm.</p></dd><dt>f.</dt><dd><p class="no_top_margin">The peaks can be further separated by dual-gradient, reversed-phase HPLC (<a class="bk_pop" href="#g19-methodglycans.REF.5">5</a>) for structural characterization (<a class="figpopup" href="/books/NBK593973/figure/g19-methodglycans.F2/?report=objectonly" target="object" rid-figpopup="figg19methodglycansF2" rid-ob="figobg19methodglycansF2">Figure 2</a>) (<a class="bk_pop" href="#g19-methodglycans.REF.3">3</a>) (<b>Note 8</b>).</p><p>The elution condition (% of dual-gradient reversed-phase B buffer, 0.2 mL/min at 25&#x000b0;C):</p><p>0&#x02013;10 min, isocratic 1%;</p><p>10&#x02013;110 min, 1%&#x02013;70%;</p><p>110.1&#x02013;120 min, isocratic 70%;</p><p>120.1&#x02013;150 min, isocratic 1%.</p><p>Emission wavelength: 400 nm and Excitation wavelength: 320 nm.</p></dd></dl></dd></dl></div><div id="g19-methodglycans.Notes"><h3>Notes</h3><p>1. Make PA freshly or store at &#x02212;30&#x000b0;C and use within a month.</p><p>2. Make freshly.</p><p>3. Forty percent ACN is sufficient to elute FNGs smaller than tri-sialyl FNGs, while it is essential to increase the ACN to 50% to elute tetra-sialyl FNGs. The increase in ACN will also elute unwanted salt, which influences the result, so it is recommended to maintain the ACN at a low concentration if the sample is expected to contain FNGs smaller than tri-sialyl glycans.</p><p>4. Serum with volume from 100 &#x003bc;L to 1 mL could be used for this analysis. The incubation time is critical for analysis as longer incubation will cause precipitation of the glycans.</p><p>5. Add 200 &#x003bc;L of dH2O, and dry the sample once again, if there is still some salt remaining in the tube.</p><p>6. Dry the sample completely. The remaining water may cause enhanced epimerization upon PA-labeling, which could artificially change the reducing-terminal glycan during the labeling process.</p><p>7. The condition for sialidase treatment is as follows: Add 10 &#x003bc;L of the PA-labeled sample with 1 &#x003bc;L of the reaction buffer and 0.5 &#x003bc;L of Sialidase and incubate overnight at 37&#x000b0;C. After the reaction, boil the reaction solution at 95&#x000b0;C for 5 min, precipitate the protein as Steps 1a&#x02013;c, and redissolve it in 10 &#x003bc;L of dH<sub>2</sub>O for HPLC analysis.</p><p>8. The condition for JB man&#x02019;ase treatment is the same as the sialidase treatment, except the fact that JB man&#x02019;ase is added instead of sialidase.</p></div></div><div id="g19-methodglycans.References"><h2 id="_g19-methodglycans_References_">References</h2><dl class="temp-labeled-list"><dt>1.</dt><dd><div class="bk_ref" id="g19-methodglycans.REF.1">Iwatsuka K, Watanabe S, Kinoshita M, Kamisue K, Yamada K, Hayakawa T, Suzuki T, Kakehi K. Free glycans derived from glycoproteins present in human sera. <span><span class="ref-journal">J Chromatogr B Analyt Technol Biomed Life Sci. </span>2013 Jun 1;<span class="ref-vol">928</span>:1621.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/23584042" ref="pagearea=cite-ref&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubmed">PubMed<span class="bk_prnt">: 23584042</span></a>] [<a href="http://dx.crossref.org/10.1016/j.jchromb.2013.03.010" ref="pagearea=cite-ref&amp;targetsite=external&amp;targetcat=link&amp;targettype=uri">CrossRef</a>]</div></dd><dt>2.</dt><dd><div class="bk_ref" id="g19-methodglycans.REF.2">Seino J, Fujihira H, Nakakita SI, Masahara-Negishi Y, Miyoshi E, Hirabayashi J, Suzuki T. Occurrence of free sialyl oligosaccharides related to N-glycans (sialyl free N-glycans) in animal sera. <span><span class="ref-journal">Glycobiology. </span>2016 Oct;<span class="ref-vol">26</span>(10):10721085.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/27102284" ref="pagearea=cite-ref&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubmed">PubMed<span class="bk_prnt">: 27102284</span></a>] [<a href="http://dx.crossref.org/10.1093/glycob/cww048" ref="pagearea=cite-ref&amp;targetsite=external&amp;targetcat=link&amp;targettype=uri">CrossRef</a>]</div></dd><dt>3.</dt><dd><div class="bk_ref" id="g19-methodglycans.REF.3">Huang C, Seino J, Fujihira H, Sato K, Fujinawa R, Sumer-Bayraktar Z, Ishii N, Matsuo I, Nakaya S, Suzuki T. Occurrence of free N-glycans with a single GlcNAc at the reducing termini in animal sera. Glycobiology. 2021 Dec 3:cwab124. doi: 10.1093/glycob/cwab124. PMID: 34939097. [<a href="https://pubmed.ncbi.nlm.nih.gov/34939097" ref="pagearea=cite-ref&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubmed">PubMed<span class="bk_prnt">: 34939097</span></a>] [<a href="http://dx.crossref.org/10.1093/glycob/cwab124" ref="pagearea=cite-ref&amp;targetsite=external&amp;targetcat=link&amp;targettype=uri">CrossRef</a>]</div></dd><dt>4.</dt><dd><div class="bk_ref" id="g19-methodglycans.REF.4">Hirayama H, Seino J, Kitajima T, Jigami Y, Suzuki T. Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae. <span><span class="ref-journal">J Biol Chem. </span>2010 Apr 16;<span class="ref-vol">285</span>(16):12390404.</span> [<a href="/pmc/articles/PMC2852977/" ref="pagearea=cite-ref&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pmc">PMC free article<span class="bk_prnt">: PMC2852977</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/20150426" ref="pagearea=cite-ref&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubmed">PubMed<span class="bk_prnt">: 20150426</span></a>] [<a href="http://dx.crossref.org/10.1074/jbc.M109.082081" ref="pagearea=cite-ref&amp;targetsite=external&amp;targetcat=link&amp;targettype=uri">CrossRef</a>]</div></dd><dt>5.</dt><dd><div class="bk_ref" id="g19-methodglycans.REF.5">Suzuki T, Matsuo I, Totani K, Funayama S, Seino J, Taniguchi N, Ito Y, Hase S. Dual-gradient high-performance liquid chromatography for identification of cytosolic high-mannose-type free glycans. <span><span class="ref-journal">Anal Biochem. </span>2008 Oct 15;<span class="ref-vol">381</span>(2):22432.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/18656438" ref="pagearea=cite-ref&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubmed">PubMed<span class="bk_prnt">: 18656438</span></a>] [<a href="http://dx.crossref.org/10.1016/j.ab.2008.07.002" ref="pagearea=cite-ref&amp;targetsite=external&amp;targetcat=link&amp;targettype=uri">CrossRef</a>]</div></dd></dl></div><h2 id="NBK593973_footnotes">Footnotes</h2><dl class="temp-labeled-list small"><dt></dt><dd><div id="g19-methodglycans.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="g19-methodglycans.F1" class="figure bk_fig"><div class="graphic"><img src="/books/NBK593973/bin/g19-methodglycans-Image001.jpg" alt="Figure 1: . Diethylaminoethanol (DEAE) anion-exchange high-performance liquid chromatography HPLC of the GC purified adult bovine serum compared with the previous purification method by amicon (2)." /></div><h3><span class="label">Figure 1: </span></h3><div class="caption"><p>Diethylaminoethanol (DEAE) anion-exchange high-performance liquid chromatography HPLC of the GC purified adult bovine serum compared with the previous purification method by amicon (<a class="bk_pop" href="#g19-methodglycans.REF.2">2</a>, <a class="bk_pop" href="#g19-methodglycans.REF.3">3</a>). Upper two panels, GC column purified adult bovine serum and the sialidase-treated control. Lower two panels, the previous Amicon (<a class="bk_pop" href="#g19-methodglycans.REF.2">2</a>) purification method purified sample and sialidase-treated control. Sialidase treated sample was analyzed simultaneously to show the sialyl glycans; note the small-sia glycans in the GC column purified sample that could not be detected by the amicon method.</p></div></div></div><div class="whole_rhythm bk_prnt_obj"><div id="g19-methodglycans.F2" class="figure bk_fig"><div class="graphic"><img src="/books/NBK593973/bin/g19-methodglycans-Image002.jpg" alt="Figure 2: . Dual-gradient reversed-phase high-performance liquid chromatography (HPLC) of flowthrough (FL) fraction from the diethylaminoethanol (DEAE) anion-exchange HPLC from GC column purified adult bovine serum (upper) and JB man&#x02019;ase-treated control (lower) (3)." /></div><h3><span class="label">Figure 2: </span></h3><div class="caption"><p>Dual-gradient reversed-phase high-performance liquid chromatography (HPLC) of flowthrough (FL) fraction from the diethylaminoethanol (DEAE) anion-exchange HPLC from GC column purified adult bovine serum (upper) and JB man&#x02019;ase-treated control (lower) (<a class="bk_pop" href="#g19-methodglycans.REF.3">3</a>). The oligomannose-type FNGs peaks sensitive to JB man&#x02019;ase treatment are indicated by black arrows, and the elution position of ManGlcNAc and ManGlcNAc<sub>2</sub> after the JB Man&#x02019;ase are shown by dotted lines. Green circle, mannose (Man); blue square, <i>N</i>-acetylglucosamine (GlcNAc).</p></div></div></div></div><div id="bk_toc_contnr"></div></div></div>
<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&amp;targetsite=external&amp;targetcat=link&amp;targettype=uri">http://creativecommons.org/licenses/by-nc-nd/4.0/</a>.</p></div><div class="small"><span class="label">Bookshelf ID: NBK593973</span><span class="label">PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/37590704" title="PubMed record of this page" ref="pagearea=meta&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubmed">37590704</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/g18-prephumanmilk/" title="Previous page in this title">&lt; Prev</a><a class="active page_link next" href="/books/n/glycopodv2/g20-prepmammal/" title="Next page in this title">Next &gt;</a></div></div></div></div>
</div>
</div>
</div>
<div class="bottom">
<div id="NCBIFooter_dynamic">
<!--<component id="Breadcrumbs" label="breadcrumbs"/>
<component id="Breadcrumbs" label="helpdesk"/>-->
</div>
<script type="text/javascript" src="/portal/portal3rc.fcgi/rlib/js/InstrumentNCBIBaseJS/InstrumentPageStarterJS.js"> </script>
</div>
</div>
<!--/.page-->
</div>
<!--/.wrap-->
</div><!-- /.twelve_col -->
</div>
<!-- /.grid -->
<span class="PAFAppResources"></span>
<!-- BESelector tab -->
<noscript><img alt="statistics" src="/stat?jsdisabled=true&amp;ncbi_db=books&amp;ncbi_pdid=book-part&amp;ncbi_acc=NBK593973&amp;ncbi_domain=glycopodv2&amp;ncbi_report=printable&amp;ncbi_type=fulltext&amp;ncbi_objectid=&amp;ncbi_pcid=/NBK593973/?report=printable&amp;ncbi_app=bookshelf" /></noscript>
<!-- usually for JS scripts at page bottom -->
<!--<component id="PageFixtures" label="styles"></component>-->
<!-- CE8B5AF87C7FFCB1_0191SID /projects/books/PBooks@9.11 portal107 v4.1.r689238 Tue, Oct 22 2024 16:10:51 -->
<span id="portal-csrf-token" style="display:none" data-token="CE8B5AF87C7FFCB1_0191SID"></span>
<script type="text/javascript" src="//static.pubmed.gov/portal/portal3rc.fcgi/4216699/js/3879255/4121861/3501987/4008961/3893018/3821238/3400083/3426610.js" snapshot="books"></script></body>
</html>