Papain-Solubilized HL-A Antigens from Cultured Human Lymphocytes Contain Two Peptide Fragments
Abstract
HL-A 2 and HL-A 7 antigens have been solubilized from cultured human lymphocytes by papain and purified on a small radioactive scale after formation of immune complexes, or on a large scale by column chromatographic methods. In both cases, it has been shown that the materials obtained consist of two noncovalently bound fragments. One fragment is a glycopeptide of molecular weight 30,000-31,000, the other is a peptide of molecular weight 11,000-12,000. In polyacrylamide gels containing 8 M urea, the large fragments of HL-A 2 and HL-A 7 exhibited different electrophoretic mobilities, while the small fragments were the same. The relationship of these materials to the native HL-A molecule is discussed.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- May 1973
- DOI:
- 10.1073/pnas.70.5.1603
- Bibcode:
- 1973PNAS...70.1603C