We have located links that may give you full text access.
Lectin Affinity Chromatography (LAC).
Many proteins are glycosylated, that is to say they have bound sugars or glycans. Glycosylation is a non-template-driven posttranslation modification. It is now known that correct glycosylation is essential for the correct folding, solubility, stability, and immunogenicity of proteins. Here, we describe the technique of Lectin Affinity Chromatography (LAC), a procedure that has the ability to separate different glycans which are attached to proteins or lipids, termed glycoproteins or glycolipids, respectively. This method utilizes different immobilized lectins that have affinity for specific sugar substrates, to separate a wide range of glycan-attached complexes (Ambrosi et al., Org Biomol Chem 3:1593-1608, 2005). To further enhance the specificity of LAC, a corresponding free sugar may be used to produce a specific elution. In general, the conditions under which lectin affinity chromatography operates are relatively mild resulting in good biological recoveries of the glycoproteins.
Full text links
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app