期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:1973
卷号:70
期号:5
页码:1603-1607
DOI:10.1073/pnas.70.5.1603
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要: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.