The Purification of Detergent-Solubilized HL-A Antigens by Affinity Chromatography with the Hemagglutinin from Lens Culinaris

[摘要] The hemagglutinin from Lens culinaris (LcH) when covalently bound to CNBr-activated Sepharose 4B is capable of binding 75 to 80% of the HL-A serologic activity solubilized from tissue culture cells with sodium deoxycholate (DOC). Serologically specific HL-A antigens may be recovered in highly purified form by elution of the bound antigens from LcH-Sepharose columns with buffer containing α-methylglucopyranose. In some experiments up to 25% of the serologic activity is not bound to the LcH-Sepharose columns and is also not bound when reapplied to freshly prepared or re-equilibrated LcH-Sepharose columns. This finding indicates that there may be an additional form of the HL-A antigen which lacks carbohydrate or contains a carbohydrate moiety not bound by LcH.

[学科分类] 生物科学（综合）