The action of alpha interferon (IFN-α) is initiated by its binding to a specific cell-surface glycoprotein, the IFN-α receptor, which is not well characterized. IFN-αA was reacted with an 125I-labeled, cleavable, heterobifunctional reagent. The derivatized IFN-αA was bound to human Daudi cells and photoactivated, forming a covalent IFN/receptor complex of apparent molecular weight 130,000-140,000 by SDS-polyacrylamide gel electrophoresis. Cleavage of the complex produced a new 125I-labeled 110 kDa band, representing the 125I-labeled IFN-α receptor free of IFN-α. This result provides a better estimate of the apparent molecular weight of the IFN-α receptor, and also provides a tool for tracking the migration of the free receptor in SDS-polyacrylamide gel electrophoresis.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Dec 30 1988|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology