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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Strominger, J. L. Cresswell, P. Turner, M. J. |
| 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. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 5 |
| Volume Number | 70 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1973-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Histocompatibility Antigens Lymphocytes Immunology Papain Pharmacology Peptides Antigen-Antibody Complex Cells, Cultured Centrifugation, Density Gradient Chromatography, Gel Electrophoresis, Polyacrylamide Gel Glucosamine Metabolism Glycopeptides Isolation & Purification Isotope Labeling Mannose Molecular Weight Sodium Dodecyl Sulfate Solubility Tritium Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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