The purification of detergent-solubilized HL-A antigens by affinity chromatography with the hemagglutinin from Lens culinaris.

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.

• Publication year

  1974

• Venue

  Journal of Immunology

• Publication date

  1974-03-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.4049/jimmunol.112.3.1190PMID 4811965
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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