Human Ia alpha- and beta-chains are sulfated
| Autor: | A J Sant, M Zacheis, T Rumbarger, K S Giacoletto, B D Schwartz |
|---|---|
| Rok vydání: | 1988 |
| Předmět: | |
| Zdroj: | The Journal of Immunology. 140:155-160 |
| ISSN: | 1550-6606 0022-1767 |
| DOI: | 10.4049/jimmunol.140.1.155 |
| Popis: | The human Ia antigens (DR, DQ, and DP), determined by genes with the HLA complex, are heterodimers consisting of a 34,000-Da alpha-chain glycoprotein and a 29,000-Da beta-chain glycoprotein. During the course of studies characterizing a recently described sulfated proteoglycan that is specifically associated with Ia, we discovered that there were also nonproteoglycan sulfated components present in the Ia immunoprecipitates. One-dimensional sodium dodecyl sulfate-gel analysis of these latter sulfated components derived from both DR and DQ immunoprecipitates indicated that these components have mobilities indistinguishable from conventional Ia alpha and beta glycoproteins. Two-dimensional gel analysis confirmed these findings and revealed that Ia-associated invariant proteins are sulfated as well. The sulfate moiety was not removed by endoglycosidase F treatment, suggesting that the protein portion of the molecule was sulfated. These results indicate that Ia alpha-, beta-, and invariant chains can be sulfated and raise the possibility that sulfation may play a role in the physiology of Ia molecules. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|