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Purification of HL-A Antigens from Normal Serum¹

Department of Surgery, School of Medicine, University of California, Los Angeles, California 90024

Abstract

A relatively simple procedure using non-denaturing techniques has been established to isolate HL-A antigens from serum. The procedure involves QAE Sephadex ion-exchange chromatography, Concanavalin A Sepharose 4B chromatography, and preparative polyacrylamide gel electrophoresis. There is approximately 17% recovery of the antigenic material in the final preparation with a 120-fold increase in specific activity over the original serum. The serum HL-A antigen is a glycoprotein containing 10 to 12% carbohydrate and having an approximate molecular weight of 130,000. The final antigen preparation migrates on polyacrylamide gels as a single band in the region of serum B₁ globulins which can be entirely removed by pretreatment with specific HL-A antibodies.

Footnotes

¹ This work was supported in part by Research Grant AM 02375 from the National Institutes of Health.