Editing Affinity chromatography (section)

===Lectins===
[[Lectin]] affinity chromatography is a form of affinity chromatography where [[lectin]]s are used to separate components within the sample. Lectins, such as [[concanavalin A]] are proteins which can bind specific alpha-D-mannose and alpha-D-glucose carbohydrate molecules. Some common carbohydrate molecules that is used in lectin affinity chromatography are Con A-Sepharose and WGA-agarose.<ref name="Freeze Unit 9.1">{{Cite book|last=Freeze|first=H. H.|date=May 2001|chapter=Lectin affinity chromatography|title=Current Protocols in Protein Science |pages=9.1.1–9.1.9|doi=10.1002/0471140864.ps0901s00|issn=1934-3663|pmid=18429210|isbn=978-0471140863|s2cid=3197260}}</ref> Another example of a lectin is wheat germ agglutinin which binds D-N-acetyl-glucosamine.<ref name="Hage 1999">{{Cite journal|last=Hage|first=David|date=May 1999|title=Affinity Chromatography: A Review of Clinical Applications|url=http://clinchem.aaccjnls.org/content/clinchem/45/5/593.full.pdf|journal=Clinical Chemistry|volume=45|issue=5|pages=593–615|pmid=10222345|doi=10.1093/clinchem/45.5.593|doi-access=free}}</ref> The most common application is to separate [[glycoprotein]]s from non-glycosylated proteins, or one [[glycoform]] from another glycoform.<ref>{{cite web|url=http://www.gelifesciences.com/aptrix/upp01077.nsf/Content/protein_purification~affinity~immobilized_lectin|title=GE Healthcare Life Sciences, Immobilized lectin|access-date=2010-11-29|archive-url=https://web.archive.org/web/20120303220910/http://www.gelifesciences.com/aptrix/upp01077.nsf/Content/protein_purification~affinity~immobilized_lectin|archive-date=2012-03-03|url-status=dead}}</ref> Although there are various ways to perform lectin affinity chromatography, the goal is extract a sugar ligand of the desired protein.<ref name="Freeze Unit 9.1"/>