Affinity chromatography of glycopeptides using concanavalin A.
作者： Milan Tomana , William Niedermeier , Jiri Mestecky , Ralph E. Schrohenloher , Sandra Porch
DOI: 10.1016/0003-2697(76)90546-7
关键词: Affinity chromatography 、 Chemistry 、 Chromatography 、 Concanavalin A 、 Glycopeptide 、 Biochemistry 、 Homogeneous 、 Sodium dodecyl sulfate 、 Polyacrylamide gel electrophoresis 、 Pronase digestion
摘要: Abstract A technique has been developed that utilizes affinity chromatography on Concanavalin (Con A)-agarose column for isolation of glycopeptides from IgA protein. Three thus obtained were homogeneous when examined by polyacrylamide gel electrophoresis in the presence sodium dodecyl sulfate. One glycopeptide contained two oligosaccharides which partially resolved following pronase digestion. Recovery applied to Con was virtually complete. The specificity present 1 protein demonstrated.
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