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<title>Binding assay of calreticulin using isothermal titration calorimetry - 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="Binding assay of calreticulin using isothermal titration calorimetry" /><meta name="citation_publisher" content="Japan Consortium for Glycobiology and Glycotechnology" /><meta name="citation_date" content="2022/03/27" /><meta name="citation_author" content="Ichiro Matsuo" /><meta name="citation_author" content="Yoichi Takeda" /><meta name="citation_pmid" content="37590773" /><meta name="citation_fulltext_html_url" content="https://www.ncbi.nlm.nih.gov/books/NBK594051/" /><meta name="citation_keywords" content="isothermal titration calorimetry" /><meta name="citation_keywords" content="monoglucosylated high-mannose type N-glycan" /><meta name="citation_keywords" content="lectin chaperone" /><link rel="schema.DC" href="http://purl.org/DC/elements/1.0/" /><meta name="DC.Title" content="Binding assay of calreticulin using isothermal titration calorimetry" /><meta name="DC.Type" content="Text" /><meta name="DC.Publisher" content="Japan Consortium for Glycobiology and Glycotechnology" /><meta name="DC.Contributor" content="Ichiro Matsuo" /><meta name="DC.Contributor" content="Yoichi Takeda" /><meta name="DC.Date" content="2022/03/27" /><meta name="DC.Identifier" content="https://www.ncbi.nlm.nih.gov/books/NBK594051/" /><meta name="description" content="Calreticulin (CRT), which is also known as a Ca2+ storage protein, acts as a lectin chaperone found in the endoplasmic reticulum (ER) of eukaryotes. It recognizes monoglucosylated oligo- mannose-type N-glycan (Glc1Man9~7GlcNAc2) on nascent polypeptide and minimizes the formation and accumulation of misfolded glycoproteins. However, the affinity of CRT for these monoglucosylated glycans is different. Isothermal titration calorimetry (ITC) is suitable for the direct detection of interactions between nonlabeled biomolecules and has been used for the analysis of various lectin–glycan interactions. It can measure the binding affinity and thermodynamic properties, such as ∆H and ΔS, in a single experiment without any chemical modification or immobilization." /><meta name="og:title" content="Binding assay of calreticulin using isothermal titration calorimetry" /><meta name="og:type" content="book" /><meta name="og:description" content="Calreticulin (CRT), which is also known as a Ca2+ storage protein, acts as a lectin chaperone found in the endoplasmic reticulum (ER) of eukaryotes. It recognizes monoglucosylated oligo- mannose-type N-glycan (Glc1Man9~7GlcNAc2) on nascent polypeptide and minimizes the formation and accumulation of misfolded glycoproteins. However, the affinity of CRT for these monoglucosylated glycans is different. Isothermal titration calorimetry (ITC) is suitable for the direct detection of interactions between nonlabeled biomolecules and has been used for the analysis of various lectin–glycan interactions. It can measure the binding affinity and thermodynamic properties, such as ∆H and ΔS, in a single experiment without any chemical modification or immobilization." /><meta name="og:url" content="https://www.ncbi.nlm.nih.gov/books/NBK594051/" /><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/g104-calreticulinITC/" /><link rel="canonical" href="https://www.ncbi.nlm.nih.gov/books/NBK594051/" /><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>
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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="_NBK594051_"><span class="title" itemprop="name">Binding assay of calreticulin using isothermal titration calorimetry</span></h1><div class="contrib half_rhythm"><span itemprop="author">Ichiro Matsuo</span>, Ph.D.<div class="affiliation small">Division of Molecular Science, Gunma University<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="pj.ca.u-amnug@oustam" class="oemail">pj.ca.u-amnug@oustam</a></div></div><div class="small">Corresponding author.</div></div><div class="contrib half_rhythm"><span itemprop="author">Yoichi Takeda</span>, Ph.D.<div class="affiliation small">Department of Biotechnology, College of Life Sciences,
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Ritsumeikan University</div></div><p class="small">Created: <span itemprop="datePublished">October 4, 2021</span>; Last Revision: <span itemprop="dateModified">March 27, 2022</span>.</p></div><div class="body-content whole_rhythm" itemprop="text"><div id="g104-calreticulinITC.Introduction"><h2 id="_g104-calreticulinITC_Introduction_">Introduction</h2><p>Calreticulin (CRT), which is also known as a Ca<sup>2+</sup> storage protein, acts as a lectin chaperone found in the endoplasmic reticulum (ER) of eukaryotes. It recognizes monoglucosylated oligo- mannose-type <i>N</i>-glycan (Glc<sub>1</sub>Man<sub>9~7</sub>GlcNAc<sub>2</sub>) on nascent polypeptide and minimizes the formation and accumulation of misfolded glycoproteins. However, the affinity of CRT for these monoglucosylated glycans is different. Isothermal titration calorimetry (ITC) is suitable for the direct detection of interactions between nonlabeled biomolecules and has been used for the analysis of various lectin–glycan interactions. It can measure the binding affinity and thermodynamic properties, such as ∆<i>H</i> and Δ<i>S</i>, in a single experiment without any chemical modification or immobilization.</p></div><div id="g104-calreticulinITC.Protocol"><h2 id="_g104-calreticulinITC_Protocol_">Protocol</h2><p>In this chapter, the protocol for binding assay will be described for the determination of binding affinity between CRT and synthetic glycan (<a class="bk_pop" href="#g104-calreticulinITC.REF.1">1</a>–<a class="bk_pop" href="#g104-calreticulinITC.REF.5">5</a>).</p><div id="g104-calreticulinITC.Materials"><h3>Materials</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Buffer A (10 mM of MOPS, 5 mM of CaCl<sub>2</sub>, and 150 mM of NaCl, pH 7.4.)</p></dd><dt>2.</dt><dd><p class="no_top_margin">2 mL of 30 μM of GST-CRT solution in buffer A</p></dd><dt>3.</dt><dd><p class="no_top_margin">400 μL of 300 μM of oligosaccharide solution in buffer A</p></dd></dl></div><div id="g104-calreticulinITC.Instruments"><h3>Instruments</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">VP-ITC calorimeter (Malvern Panalytical Ltd., Worcestershire, UK) (<b>Note 1</b>).</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">VP-ITC Cell (sample cell)</p></dd><dt>b.</dt><dd><p class="no_top_margin">Auto Pipette (injection syringe)</p></dd></dl></dd><dt>2.</dt><dd><p class="no_top_margin">Hamilton 2.5-mL filling syringe</p></dd><dt>3.</dt><dd><p class="no_top_margin">Plastic syringe (1 mL)</p></dd><dt>4.</dt><dd><p class="no_top_margin">UV-visible spectrometer</p></dd><dt>5.</dt><dd><p class="no_top_margin">Refrigerated centrifuge</p></dd><dt>6.</dt><dd><p class="no_top_margin">10 kDa Amicon Ultra (10 K) Centrifugal Filter Unit</p></dd></dl></div><div id="g104-calreticulinITC.Methods"><h3>Methods</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Protocol for the preparation of protein sample</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">GST-CRT was dialyzed against buffer A at least three times and concentrated using 10 kDa Amicon Ultra Centrifugal Filter Unit.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Protein concentration of GST-CRT was determined by A280 as 1.06 (1 mg/mL).</p></dd><dt>c.</dt><dd><p class="no_top_margin">2 mL of protein solution was prepared (the final concentration was adjusted at 30 μM) (<b>Note 2</b>).</p></dd><dt>d.</dt><dd><p class="no_top_margin">The protein solution was degassed under vacuum (strength of vacuum needs to be adjusted based on the behavior of the samples under vacuum).</p></dd></dl></dd><dt>2.</dt><dd><p class="no_top_margin">Protocol for the preparation of oligosaccharide sample</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">1 mg of Glc<sub>1</sub>Man<sub>9</sub>GlcNAc<sub>2</sub>-OC<sub>3</sub>H<sub>7</sub> was dissolved 1 mL of buffer A (500 μM).</p></dd><dt>b.</dt><dd><p class="no_top_margin">250 μL of the Glc<sub>1</sub>Man<sub>9</sub>GlcNAc<sub>2</sub>-OC<sub>3</sub>H<sub>7</sub> solution was added to 150 μL of buffer A (the final concentration was adjusted at 300 μM) (<b>Note 3</b>).</p></dd><dt>c.</dt><dd><p class="no_top_margin">The oligosaccharide solution was degassed under vacuum (strength of vacuum needs to be adjusted based on the behavior of the samples under vacuum).</p></dd></dl></dd><dt>3.</dt><dd><p class="no_top_margin">Performing an experiment and data analysis</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Slowly draw a minimum 1.8 mL of the protein solution into the filling syringe.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Remove all air from the filling syringe.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Insert the syringe into the sample cell and slowly inject the protein solution.</p></dd><dt>d.</dt><dd><p class="no_top_margin">Remove bubbles in the sample cell and adjust the sample volume to 1.4181 mL (<b>Note 4</b>).</p></dd><dt>e.</dt><dd><p class="no_top_margin">Load the oligosaccharide solution (300 μL) into the Auto Pipette using a plastic syringe.</p></dd><dt>f.</dt><dd><p class="no_top_margin">Carefully insert the Auto Pipette into the sample cell with a spinning rate of 300 rpm at 25°C.</p></dd><dt>g.</dt><dd><p class="no_top_margin">The oligosaccharide solution was added as 50 injections of 6 μL into the sample cell (an interval of 3 min between each injection) (<b>Note 5</b>).</p></dd><dt>h.</dt><dd><p class="no_top_margin">Titration data as shown in <a class="figpopup" href="/books/NBK594051/figure/g104-calreticulinITC.F1/?report=objectonly" target="object" rid-figpopup="figg104calreticulinITCF1" rid-ob="figobg104calreticulinITCF1">Figure 1</a> were fitted using the one set of site method to determine binding stoichiometry (n), binding constant (KA) (<a class="figpopup" href="/books/NBK594051/figure/g104-calreticulinITC.F2/?report=objectonly" target="object" rid-figpopup="figg104calreticulinITCF2" rid-ob="figobg104calreticulinITCF2">Figure 2</a>), and change in enthalpy of binding (Δ<i>H</i>) using Origin software (MicroCal).</p></dd></dl></dd></dl></div><div id="g104-calreticulinITC.Notes"><h3>Notes</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">The VP-ITC is not currently for sale, and the current type MicroCal PEAQ-ITC is for sale by Malvern Panalytical Ltd. The PEAQ-ITC has a cell capacity of 200 µL (required capacity of 280 µL) and a syringe capacity of 40 µL, which can significantly reduce sample consumption compared to VP-ITC. Additionally, degassing of sample solution is usually not required, and filling of ligand solution is automated, eliminating the need for complex operations.</p></dd><dt>2.</dt><dd><p class="no_top_margin">A favorable concentration of lectin depends on KA, n, and ΔH (heat change in cal/mole). The unitless constant, c, which is derived by Wiseman et al. (<a class="bk_pop" href="#g104-calreticulinITC.REF.7">6</a>), is useful for experimental design.</p><ul class="simple-list"><li class="half_rhythm"><div>c = n × [P] × KA</div></li><li class="half_rhythm"><div>When c ranges from 5 to 250, a sigmoidal thermogram will be obtained, which provides accurate estimates of KA.</div></li></ul></dd><dt>3.</dt><dd><p class="no_top_margin">If a glycan sample that cannot be weighed on a balance, it should be quantified by the phenol–sulfuric acid method (<a class="bk_pop" href="#g104-calreticulinITC.REF.7">7</a>) using concentrated sulfuric acid (Sigma-Aldrich) and 5% aqueous phenol solution, which is prepared by adding 5 g of redistilled reagent grade phenol (Sigma-Aldrich) to 95 g of ultrapure water.</p></dd><dt>4.</dt><dd><p class="no_top_margin">Dust, other particulates, and air bubbles can cause artifacts in the baseline of the ITC thermogram. The sample should be centrifuged in microcentrifuge tubes to remove pellet particles.</p></dd><dt>5.</dt><dd><p class="no_top_margin">Control experiments should be conducted by injecting the glycan solution into the buffer.</p></dd></dl></div></div><div id="g104-calreticulinITC.References"><h2 id="_g104-calreticulinITC_References_">References</h2><dl class="temp-labeled-list"><dt>1.</dt><dd><div class="bk_ref" id="g104-calreticulinITC.REF.1">Matsuo I, Totani K, Tatami A, Ito Y. Comprehensive synthesis of ER related high-mannose-type sugar chains by convergent strategy. <span><span class="ref-journal">Tetrahedron. </span>2006 Aug 28;<span class="ref-vol">62</span>(35):8262–77.</span> [<a href="http://dx.crossref.org/10.1016/j.tet.2006.06.045" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>2.</dt><dd><div class="bk_ref" id="g104-calreticulinITC.REF.2">Matsuo I, Wada M, Manabe S, Yamaguchi Y, Otake K, et al. Synthesis of monoglucosylated high-mannose-type dodecasaccharide, a putative ligand for molecular chaperone, calnexin, and calreticulin. <span><span class="ref-journal">J Am Chem Soc. </span>2003 Feb 28;<span class="ref-vol">125</span>(12):3402–3403.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/12643681" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 12643681</span></a>] [<a href="http://dx.crossref.org/10.1021/ja021288q" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>3.</dt><dd><div class="bk_ref" id="g104-calreticulinITC.REF.3">Arai MA, Matsuo I, Hagihara S, Totani K, Maruyama J, et al. Design and synthesis of oligosaccharides that interfere with glycoprotein quality-control systems. <span><span class="ref-journal">Chembiochem. </span>2005 Nov 30;<span class="ref-vol">6</span>(12):2281–89.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/16283686" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 16283686</span></a>] [<a href="http://dx.crossref.org/10.1002/cbic.200500143" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>4.</dt><dd><div class="bk_ref" id="g104-calreticulinITC.REF.4">Ito Y, Hagihara S, Arai MA, Matsuo I, Takatani M. Synthesis of fluorine substituted oligosaccharide analogues of monoglucosylated glycan chain, a proposed ligand of lectin-chaperone calreticulin and calnexin. <span><span class="ref-journal">Glycoconjugate J. </span>2004 Sep;<span class="ref-vol">21</span>(5):257–66.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/15486458" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 15486458</span></a>] [<a href="http://dx.crossref.org/10.1023/B:GLYC.0000045109.60425.2e" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>5.</dt><dd><div class="bk_ref" id="g104-calreticulinITC.REF.5">Ito Y, Hagihara S, Matsuo I, Totani K. Structural approaches to the study of oligosaccharides in glycoprotein quality control. <span><span class="ref-journal">Curr Opin Struct Biol. </span>2005 Sep 9;<span class="ref-vol">15</span>:481–89.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/16154739" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 16154739</span></a>] [<a href="http://dx.crossref.org/10.1016/j.sbi.2005.08.012" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>6.</dt><dd><div class="bk_ref" id="g104-calreticulinITC.REF.6">Wiseman T, Williston S, Brandts JF, Lin LN. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. <span><span class="ref-journal">Anal Biochem. </span>1989 May 15;<span class="ref-vol">179</span>(1):131–7.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/2757186" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 2757186</span></a>] [<a href="http://dx.crossref.org/10.1016/0003-2697(89)90213-3" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>7.</dt><dd><div class="bk_ref" id="g104-calreticulinITC.REF.7">Saha AK, Brewer CF. Determination of the concentrations of oligosaccharides, complex type carbohydrates, and glycoproteins using the phenol-sulfuric acid method. <span><span class="ref-journal">Carbohydr Res. </span>1994 Feb 17;<span class="ref-vol">254</span>:157–67.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/8180982" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 8180982</span></a>] [<a href="http://dx.crossref.org/10.1016/0008-6215(94)84249-3" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>8.</dt><dd><div class="bk_ref" id="g104-calreticulinITC.REF.8">Kapoor M, Srinivas H, Kandiah H, Gemma E, Ellgaard L, Oscarson S, Helenius A, Surolia A. Interactions of Substrate with Calreticulin, an Endoplasmic Reticulum Chaperone. <span><span class="ref-journal">J Biol Chem. </span>2003 Feb 21;<span class="ref-vol">278</span>(8):6194–200.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/12464625" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 12464625</span></a>] [<a href="http://dx.crossref.org/10.1074/jbc.M209132200" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd></dl></div><h2 id="NBK594051_footnotes">Footnotes</h2><dl class="temp-labeled-list small"><dt></dt><dd><div id="g104-calreticulinITC.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="g104-calreticulinITC.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.%20Isothermal%20titration%20calorimetry%20of%20calreticulin%20with%20A%3A%20Glc2Man9GlcNAc2-OC3H7%2C%20B%3A%20Glc1Man9GlcNAc2-OC3H7%2C%20and%20C%3A%20Man9GlcNAc2-OC3H7.&p=BOOKS&id=594051_g104-calreticulinITC-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/NBK594051/bin/g104-calreticulinITC-Image001.jpg" alt="Figure 1: . Isothermal titration calorimetry of calreticulin with A: Glc2Man9GlcNAc2-OC3H7, B: Glc1Man9GlcNAc2-OC3H7, and C: Man9GlcNAc2-OC3H7." class="tileshop" title="Click on image to zoom" /></a></div><h3><span class="label">Figure 1: </span></h3><div class="caption"><p>Isothermal titration calorimetry of calreticulin with A: Glc<sub>2</sub>Man<sub>9</sub>GlcNAc<sub>2</sub>-OC<sub>3</sub>H<sub>7</sub>, B: Glc<sub>1</sub>Man<sub>9</sub>GlcNAc<sub>2</sub>-OC<sub>3</sub>H<sub>7</sub>, and C: Man<sub>9</sub>GlcNAc<sub>2</sub>-OC<sub>3</sub>H<sub>7</sub>.</p></div></div></div><div class="whole_rhythm bk_prnt_obj"><div id="g104-calreticulinITC.F2" class="figure bk_fig"><div class="graphic"><a href="/core/lw/2.0/html/tileshop_pmc/tileshop_pmc_inline.html?title=Figure%202%3A%20.%20Binding%20of%20endoplasmic%20reticulum%20(ER)%02013related%20N-glycans%20to%20calreticulin%20(CRT).&p=BOOKS&id=594051_g104-calreticulinITC-Image002.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/NBK594051/bin/g104-calreticulinITC-Image002.jpg" alt="Figure 2: . Binding of endoplasmic reticulum (ER)–related N-glycans to calreticulin (CRT)." class="tileshop" title="Click on image to zoom" /></a></div><h3><span class="label">Figure 2: </span></h3><div class="caption"><p>Binding of endoplasmic reticulum (ER)–related <i>N</i>-glycans to calreticulin (CRT). *The binding constant of Glc1Man3 to CRT was reported by Kapoor et al. (<a class="bk_pop" href="#g104-calreticulinITC.REF.8">8</a>).</p></div></div></div></div><div id="bk_toc_contnr"></div></div></div>
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