Multiple lectin detection by cell membrane affinity binding

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• 作者：Ana Ribeiro^a ; ^b ; ^{acribeiro@ff.ul.pt} ; Sofia Catarino^b ; ^{sofiagcatarino@gmail.com} ; Ricardo Boavida Ferreira^b ; ^c ; ^{rbferreira@itqb.unl.pt}
• 关键词：GalNAc ; N-acetyl-d-galactosamine ; GlcNAc ; N-acetyl-d-glucosamine ; Neu5Ac ; N-acetylneuraminic acid (sialic acid) ; Con-A ; concanavalin A ; Fuc ; l-fucose ; GalN ; d-galactosamine ; Gal ; d-galactose ; GlcN ; d-glucosamine ; Glc ; d-glucose ; Man ; d-mannose ; Mlz ; melez
• 刊名：Carbohydrate Research
• 出版年：2012
• 期刊代码：15_00086215
• 类别：ch
• 出版时间：1 May, 2012
• 卷：352
• 期：Complete
• 页码：206-210
• 文件大小：648 K

摘要

Assuming that lectins evolved to recognise relatively complex and branched oligosaccharides or parts of them, rather than simple sugars, a procedure based on lectin affinity binding to isolated erythrocyte (or any other cell type) membranes is proposed. This methodology was validated using six pure commercial lectins, as well as lectins from total protein extracts of Arbutus unedo leaves. All commercial lectins, as well as five polypeptides from A. unedo leaves bound to the glycosylated membrane receptors and were eluted by the corresponding sugars. When compared to the standard affinity chromatography procedure involving an individual sugar bound to a solid matrix, the new method provides a single-step, effective detection method for lectins and allows the rapid screening of their profile present in any unknown protein solution, indicates their biological carbohydrate affinities as well as their sugar specificities (if any), enables the simultaneous analysis of a large number of samples, does not require any pre-purification steps, permits detection of additional lectins and provides data which are more relevant from the physiological point of view.