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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="Lectin blotting" /><meta name="citation_publisher" content="Japan Consortium for Glycobiology and Glycotechnology" /><meta name="citation_date" content="2022/03/21" /><meta name="citation_author" content="Motohiro Nonaka" /><meta name="citation_author" content="Toshisuke Kawasaki" /><meta name="citation_pmid" content="37590714" /><meta name="citation_fulltext_html_url" content="https://www.ncbi.nlm.nih.gov/books/NBK593985/" /><meta name="citation_keywords" content="lectin blotting" /><meta name="citation_keywords" content="lectin" /><meta name="citation_keywords" content="glycoproteins" /><meta name="citation_keywords" content="glycoforms" /><meta name="citation_keywords" content="sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)" /><link rel="schema.DC" href="http://purl.org/DC/elements/1.0/" /><meta name="DC.Title" content="Lectin blotting" /><meta name="DC.Type" content="Text" /><meta name="DC.Publisher" content="Japan Consortium for Glycobiology and Glycotechnology" /><meta name="DC.Contributor" content="Motohiro Nonaka" /><meta name="DC.Contributor" content="Toshisuke Kawasaki" /><meta name="DC.Date" content="2022/03/21" /><meta name="DC.Identifier" content="https://www.ncbi.nlm.nih.gov/books/NBK593985/" /><meta name="description" content="In pathological tissues and cells, glycan structures often change, even in originally identical proteins. Lectin blotting, along with Western blotting using an antibody against the target protein, not only allows the determination of the glycoforms of the new protein of interest (1–4) but also provides useful information for discriminating such changes (5,6). Lectin blotting can be performed using either gel electrophoresis (SDS-PAGE) (Figure 1) or two-dimensional (2D) gel electrophoresis (2D SDS-PAGE) followed by blotting a membrane. Although oligosaccharide is not usually affected by reducing reagents (e.g., 2-mercaptoethanol) used in the SDS-PAGE, one should consider the effect of denatured condition of the protein, which might disrupt intermolecular location of glycans, resulting in the loss of binding to lectins." /><meta name="og:title" content="Lectin blotting" /><meta name="og:type" content="book" /><meta name="og:description" content="In pathological tissues and cells, glycan structures often change, even in originally identical proteins. Lectin blotting, along with Western blotting using an antibody against the target protein, not only allows the determination of the glycoforms of the new protein of interest (1–4) but also provides useful information for discriminating such changes (5,6). Lectin blotting can be performed using either gel electrophoresis (SDS-PAGE) (Figure 1) or two-dimensional (2D) gel electrophoresis (2D SDS-PAGE) followed by blotting a membrane. Although oligosaccharide is not usually affected by reducing reagents (e.g., 2-mercaptoethanol) used in the SDS-PAGE, one should consider the effect of denatured condition of the protein, which might disrupt intermolecular location of glycans, resulting in the loss of binding to lectins." /><meta name="og:url" content="https://www.ncbi.nlm.nih.gov/books/NBK593985/" /><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/g175-lectinblot/" /><link rel="canonical" href="https://www.ncbi.nlm.nih.gov/books/NBK593985/" /><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="_NBK593985_"><span class="title" itemprop="name">Lectin blotting</span></h1><div class="contrib half_rhythm"><span itemprop="author">Motohiro Nonaka</span>, Dr.<div class="affiliation small">Kyoto University<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="pj.ca.u-otoyk@r4.orihotom.akanon" class="oemail">pj.ca.u-otoyk@r4.orihotom.akanon</a></div></div><div class="small">Corresponding author.</div></div><div class="contrib half_rhythm"><span itemprop="author">Toshisuke Kawasaki</span>, Dr.<div class="affiliation small">Ritsumeikan University<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="pj.ca.iemustir.cf@kasawakt" class="oemail">pj.ca.iemustir.cf@kasawakt</a></div></div></div><p class="small">Created: <span itemprop="datePublished">September 10, 2021</span>; Last Revision: <span itemprop="dateModified">March 21, 2022</span>.</p></div><div class="body-content whole_rhythm" itemprop="text"><div id="g175-lectinblot.Introduction"><h2 id="_g175-lectinblot_Introduction_">Introduction:</h2><p>In pathological tissues and cells, glycan structures often change, even in originally identical proteins. Lectin blotting, along with Western blotting using an antibody against the target protein, not only allows the determination of the glycoforms of the new protein of interest (<a class="bk_pop" href="#g175-lectinblot.REF.1">1</a>–<a class="bk_pop" href="#g175-lectinblot.REF.4">4</a>) but also provides useful information for discriminating such changes (<a class="bk_pop" href="#g175-lectinblot.REF.5">5</a>,<a class="bk_pop" href="#g175-lectinblot.REF.6">6</a>). Lectin blotting can be performed using either gel electrophoresis (SDS-PAGE) (<a class="figpopup" href="/books/NBK593985/figure/g175-lectinblot.F1/?report=objectonly" target="object" rid-figpopup="figg175lectinblotF1" rid-ob="figobg175lectinblotF1">Figure 1</a>) or two-dimensional (2D) gel electrophoresis (2D SDS-PAGE) followed by blotting a membrane. Although oligosaccharide is not usually affected by reducing reagents (e.g., 2-mercaptoethanol) used in the SDS-PAGE, one should consider the effect of denatured condition of the protein, which might disrupt intermolecular location of glycans, resulting in the loss of binding to lectins.</p></div><div id="g175-lectinblot.Protocol"><h2 id="_g175-lectinblot_Protocol_">Protocol</h2><p>In this chapter, we describe a lectin blotting method using biotinylated lectin followed by detection with horseradish peroxidase (HRP)-labeled Streptavidin. Here, signal amplification based on the biotin-avidin system is expected. However, if you have specific antibodies against lectins, you can also use them for detection.</p><div id="g175-lectinblot.Materials"><h3>Materials</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Purified glycoprotein or crude glycoprotein samples from cells, etc.</p></dd><dt>2.</dt><dd><p class="no_top_margin">Transfer buffer for protein blotting: 25 mM of Tris, 192 mM of glycine, and 10% methanol</p></dd><dt>3.</dt><dd><p class="no_top_margin">The nitrocellulose membranes or polyvinylidene difluoride (PVDF) membranes (Bio-Rad Laboratories, Hercules, CA)</p></dd><dt>4.</dt><dd><p class="no_top_margin">The filter papers (Whatman International Ltd., Kent, UK or Bio-Rad Laboratories)</p></dd><dt>5.</dt><dd><p class="no_top_margin">Tris-buffered saline (TBS): 137 mM of NaCl, 2.68 mM of KCl, and 25 mM of Tris-HCl, pH 7.4</p></dd><dt>6.</dt><dd><p class="no_top_margin">Phosphate-buffered saline (PBS): 137 mM of NaCl, 8.1 mM of Na<sub>2</sub>HPO<sub>4</sub>, 2.68 mM of KCl, and 1.47 mM of KH<sub>2</sub>PO<sub>4</sub>, pH 7.4</p></dd><dt>7.</dt><dd><p class="no_top_margin">Washing buffer: 0.05% (w/v) Tween-20 in TBS (TBST) or PBS (PBST)</p></dd><dt>8.</dt><dd><p class="no_top_margin">Blocking solution: 3% (w/v) bovine serum albumin (BSA) or 3% (w/v) skim milk in TBST or PBST</p></dd><dt>9.</dt><dd><p class="no_top_margin">Biotinylated lectins and HRP-labeled Streptavidin or alkaline phosphatase (AP)-labeled Streptavidin</p></dd><dt>10.</dt><dd><p class="no_top_margin">Chromogenic or luminescent visualization regent for detecting tagged lectin or antibody</p></dd><dt>11.</dt><dd><p class="no_top_margin">Two detection methods: the chemiluminescent detection of HRP activity using the luminol reagent (PIERCE Kit) and the conventional colorimetric reaction of AP revealed by nitroblue tetrazolium/bromochloro-indolyl phosphate (NBT/BCIP)</p></dd></dl></div><div id="g175-lectinblot.Instruments"><h3>Instruments</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">SDS-PAGE electrophoresis apparatus (e.g., mini-slab PAGE apparatus AE-6500, ATTO, Tokyo, Japan)</p></dd><dt>2.</dt><dd><p class="no_top_margin">Transfer apparatus (e.g., Trans-Blot® SD Semi-Dry Transfer Cell, Bio-Rad Laboratories)</p></dd><dt>3.</dt><dd><p class="no_top_margin">Image analyzer for chemiluminescence (e.g., LAS-4000, Fujifilm, Tokyo, Japan)</p></dd></dl></div><div id="g175-lectinblot.Methods"><h3>Methods</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">SDS-PAGE or 2D SDS-PAGE electrophoresis</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Prepare the glycoprotein samples.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Run on 5%–20% SDS-PAGE or 2D SDS-PAGE gel until dye front is 0.5 cm away from the bottom of the gel.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Set up the transfer apparatus.</p></dd></dl></dd><dt>2.</dt><dd><p class="no_top_margin">Protein-blotting procedures</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Prepare transfer buffer while the gel is running and degas for at least 1 h before transfer.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Remove the gel plates carefully and transfer to the container containing the transfer buffer.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Wet the transfer nitrocellulose membrane thoroughly in a small amount of methanol (<b>Note 1</b>).</p></dd><dt>d.</dt><dd><p class="no_top_margin">Wet the filter papers and the transfer membrane thoroughly in the transfer buffer.</p></dd><dt>e.</dt><dd><p class="no_top_margin">Place transfer membrane on the gel and ensure that there are no bubbles.</p></dd><dt>f.</dt><dd><p class="no_top_margin">Place the 5 wetted pieces of filter papers on the membrane and ensure that there are no bubbles.</p></dd><dt>g.</dt><dd><p class="no_top_margin">Place them on the transfer assembly.</p></dd><dt>h.</dt><dd><p class="no_top_margin">Connect the lead to the power source and transfer for 1 h.</p></dd></dl></dd><dt>3.</dt><dd><p class="no_top_margin">Lectin-blotting procedures</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">After transferring proteins from the gel to the membrane, remove the membrane and rinse briefly in TBS or water.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Treat the membrane with 15 mL blocking solution for 1 h at room temperature with gentle agitation (<b>Note 2</b>)<b>.</b></p></dd><dt>c.</dt><dd><p class="no_top_margin">Remove the blocking buffer and incubate the membrane for 1–2 h in biotinylated lectin at a concentration of 1 μg/mL in the blocking solution with agitation at room temperature. Usually, 15 mL of the lectin solution is used for incubating a membrane of 9 × 9 cm (<b>Note 3</b>).</p></dd><dt>d.</dt><dd><p class="no_top_margin">Wash the membrane at least 4 times for 5 min each with TBST.</p></dd><dt>e.</dt><dd><p class="no_top_margin">Add Streptavidin-HRP or Streptavidin-AP diluted in the blocking solution for 1 h at room temperature with agitation.</p></dd><dt>f.</dt><dd><p class="no_top_margin">Wash the membrane at least 4 times for 5 min each with TBST and then rinse twice with TBS.</p></dd><dt>g.</dt><dd><p class="no_top_margin">Perform chemiluminescence detection of peroxidase activity with a SuperSignal West Pico Chemiluminescent kit according to the manufacturer’s instructions (PIERCE). Incubate the membrane for 1 min at room temperature without agitation.</p></dd><dt>h.</dt><dd><p class="no_top_margin">Drain excess chemiluminescent solution by holding the membrane vertically. Then wrap blots in plastic sheet (Saran Wrap), without introducing air bubbles.</p></dd><dt>i.</dt><dd><p class="no_top_margin">Detect the luminescence with an automatic developer or manually by electronic imaging systems. The exposure time of the blots depends on the number of target proteins on the membrane (<b>Note 4</b>).</p></dd></dl></dd></dl></div><div id="g175-lectinblot.Notes"><h3>Notes</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Instead of nitrocellulose, PVDF membrane can be used for lectin blotting.</p></dd><dt>2.</dt><dd><p class="no_top_margin">Generally, BSA or nonfat dried skim milk is used to block membranes. For lectin blotting, we have tested BSA, which has produced a high background. When low-fat dried skim milk was used, it gave a low background for colorimetric and chemiluminescent detections. If no glycoprotein signals were obtained on the blot after the chemiluminescent reaction, this could be attributed to the presence of biotin in the skim milk that competed with biotinylated lectin and avoided its binding to the sugar moieties of glycoproteins.</p></dd><dt>3.</dt><dd><p class="no_top_margin">The blots should be immersed in a sufficient volume of solution to allow a good exchange of fluid over its entire surface. The use of plastic bags to incubate protein blots is not recommended because it often leads to uneven background and may cause areas without signal. Depending on the carbohydrate specificity of the lectin, it may be necessary to optimize working dilution. Notably, when the calcium-dependent lectins, such as C-type lectin, are used, PBS must be replaced by another buffer system, such as TBS or HEPES buffer. Then, calcium phosphate precipitation occurs.</p></dd><dt>4.</dt><dd><p class="no_top_margin">The difference in the exposure time depends on the lectin used. For example, if the lectin detects most of the <i>N</i>-linked glycoproteins, an exposure for a few seconds may be sufficient. Here, a longer exposure time leads to a high background with no additional spot signal.</p></dd></dl></div></div><div id="g175-lectinblot.References"><h2 id="_g175-lectinblot_References_">References</h2><dl class="temp-labeled-list"><dt>1.</dt><dd><div class="bk_ref" id="g175-lectinblot.REF.1">Uemura K, Yokota Y, Kozutsumi Y, Kawasaki T. A Unique CD45 Glycoform Recognized by the Serum Mannan-binding Protein in Immature Thymocytes. <span><span class="ref-journal">J Biol Chem. </span>1996 Mar 1;<span class="ref-vol">271</span>(9):4581–4.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/8617714" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 8617714</span></a>] [<a href="http://dx.crossref.org/10.1074/jbc.271.9.4581" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>2.</dt><dd><div class="bk_ref" id="g175-lectinblot.REF.2">Hirano M, Ma BY, Kawasaki N, Okimura K, Baba M, Nakagawa T, Miwa K, Kawasaki N, Oka S, Kawasaki T. Mannan-binding protein blocks the activation of metalloproteases meprin alpha and beta. <span><span class="ref-journal">J Immunol. </span>2005 Sep 1;<span class="ref-vol">175</span>(5):3177–85.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/16116208" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 16116208</span></a>] [<a href="http://dx.crossref.org/10.4049/jimmunol.175.5.3177" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>3.</dt><dd><div class="bk_ref" id="g175-lectinblot.REF.3">Yaji S, Manya H, Nakagawa N, Takematsu H, Endo T, Kannagi R, Yoshihara T, Asano M, Oka S. Major glycan structure underlying expression of the Lewis X epitope in the developing brain is O-mannose-linked glycans on phosphacan/RPTPβ. <span><span class="ref-journal">Glycobiology. </span>2015 Apr;<span class="ref-vol">25</span>(4):376–85.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/25361541" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 25361541</span></a>] [<a href="http://dx.crossref.org/10.1093/glycob/cwu118" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>4.</dt><dd><div class="bk_ref" id="g175-lectinblot.REF.4">Kouno T, Kizuka Y, Nakagawa N, Yoshihara T, Asano M, Oka S. Specific enzyme complex of β-1, 4-galactosyltransferase-II and glucuronyltransferase-P facilitates biosynthesis of N-linked human natural killer-1 (HNK-1) carbohydrate. <span><span class="ref-journal">J Biol Chem. </span>2011;<span class="ref-vol">286</span>(36):31337–46.</span> [<a href="/pmc/articles/PMC3173110/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC3173110</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/21771787" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 21771787</span></a>] [<a href="http://dx.crossref.org/10.1074/jbc.M111.233353" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>5.</dt><dd><div class="bk_ref" id="g175-lectinblot.REF.5">Nonaka M, Ma BY, Imaeda H, Kawabe K, Kawasaki N, Hodohara K, Kawasaki N, Andoh A, Fujiyama Y, Kawasaki T. Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) recognizes a novel ligand, Mac-2-binding protein, characteristically expressed on human colorectal carcinomas. <span><span class="ref-journal">J Biol Chem. </span>2011 Jun 24;<span class="ref-vol">286</span>(25):22403–13.</span> [<a href="/pmc/articles/PMC3121387/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC3121387</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/21515679" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 21515679</span></a>] [<a href="http://dx.crossref.org/10.1074/jbc.M110.215301" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>6.</dt><dd><div class="bk_ref" id="g175-lectinblot.REF.6">Kawasaki N, Lin CW, Inoue R, Khoo KH, Kawasaki N, Ma BY, Oka S, Ishiguro M, Sawada T, Ishida H, Hashimoto T, Kawasaki T. Highly fucosylated N-glycan ligands for mannan-binding protein expressed specifically on CD26 (DPPVI) isolated from a human colorectal carcinoma cell line, SW1116. <span><span class="ref-journal">Glycobiology. </span>2009 Apr;<span class="ref-vol">19</span>(4):437–50.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/19129245" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19129245</span></a>] [<a href="http://dx.crossref.org/10.1093/glycob/cwn158" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd></dl></div><h2 id="NBK593985_footnotes">Footnotes</h2><dl class="temp-labeled-list small"><dt></dt><dd><div id="g175-lectinblot.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="g175-lectinblot.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.%20Lectin%20blotting%20and%20deglycosylation%20analyses%20of%20the%20purified%20mannan-binding%20protein%20(MBP)%20ligands.&p=BOOKS&id=593985_g175-lectinblot-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/NBK593985/bin/g175-lectinblot-Image001.jpg" alt="Figure 1: . Lectin blotting and deglycosylation analyses of the purified mannan-binding protein (MBP) ligands." class="tileshop" title="Click on image to zoom" /></a></div><h3><span class="label">Figure 1: </span></h3><div class="caption"><p>Lectin blotting and deglycosylation analyses of the purified mannan-binding protein (MBP) ligands. Meprins, as novel endogenous MBP ligands, were separated and identified by affinity chromatography and mass spectrometry. To characterize the glycans expressed in meprins and to study the interaction of MBP with these glycans, oligosaccharides were enzymatically removed from meprins by <i>N</i>-glycosidase F (F) or endoglycosidase H (H). The reactivity of the deglycosylated meprins to MBP was examined by MBP-blotting and <i>Aleuria aurantia</i> Lectin (AAL)-blotting analyses. <i>N</i>-glycosidase F digests all <i>N</i>-glycans, whereas endoglycosidase H digests high-mannose and hybrid-type but not complex-type <i>N</i>-glycans. Reduced reactiveness upon treatment of those enzymes indicates that MBP binds to meprins through high-mannose or hybrid-type <i>N</i>-glycans. The finding that fucose-binding AAL lectin retains its reactivity with meprins treated with endoglycosidase H suggests that meprins have core fucose.</p></div><div class="permissions">This figure was originally published in J Immunol. Hirano M, Ma BY. et al. "Mannan-binding protein blocks the activation of metalloproteases meprin alpha and beta” 2005, 175(5):3177–85. © The American Association of Immunologists, Inc.</div></div></div></div><div id="bk_toc_contnr"></div></div></div>
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