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The Purification of Detergent-Solubilized HL-A Antigens by Affinity Chromatography with the Hemagglutinin from Lens Culinaris¹

Division of Immunology, Department of Microbiology and Immunology, Duke University Medical Center, Durham, North Carolina 27710

Abstract

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 -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.

Footnotes

¹ This work was supported by United States Public Health Service Grants AI-08897, AM-13084, and AI-18399.

² Supported by the Duke University Undergraduate Research Assistantship Program.