| Autor: |
Peterson, Per A., Rask, Lars, Lindblom, J. Bertil |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; January 1974, Vol. 71 Issue: 1 p35-39, 5p |
| Abstrakt: |
HL-A antigens comprising 11 different antigenic specificities were isolated after papain solubilization of spleen-cell membrane constituents. During the entire purification procedure, β2-microglobulin appeared together with the HL-A antigens. The highly purified antigens were composed of two polypeptide chains. The large subunit carried the antigenic specificity whereas the small polypeptide chain was very similar, if not identical, to β2-microglobulin. The two HL-A antigen polypeptide chains were held together by noncovalent interactions only, and β2-microglobulin, isolated from urine, could replace the small subunit in forming a complex with the large polypeptide chain. The topographical relationship in the cell membrane between β2-microglobulin and the large HL-A antigen polypeptide chain is unknown. The two polypeptide chains may be fortuitously bound as a result of the solubilization procedure. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
