Langer J A
Department of Molecular Genetics and Microbiology, University of Medicine and Dentistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854-5635.
Biochem Biophys Res Commun. 1988 Dec 30;157(3):1264-70. doi: 10.1016/s0006-291x(88)81011-8.
The action of alpha interferon (IFN-alpha) is initiated by its binding to a specific cell-surface glycoprotein, the IFN-alpha receptor, which is not well characterized. IFN-alpha A was reacted with an 125I-labeled, cleavable, heterobifunctional reagent. The derivatized IFN-alpha A 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-alpha receptor free of IFN-alpha. This result provides a better estimate of the apparent molecular weight of the IFN-alpha receptor, and also provides a tool for tracking the migration of the free receptor in SDS-polyacrylamide gel electrophoresis.
α干扰素（IFN-α）的作用是通过其与一种特定的细胞表面糖蛋白即IFN-α受体结合而启动的，该受体的特性尚未完全明确。将IFN-α A与一种125I标记的、可裂解的异双功能试剂反应。衍生化的IFN-α A与人Daudi细胞结合并进行光活化，通过SDS-聚丙烯酰胺凝胶电泳形成了表观分子量为130,000 - 140,000的共价IFN/受体复合物。该复合物的裂解产生了一条新的125I标记的110 kDa条带，代表不含IFN-α的125I标记的IFN-α受体。这一结果能更好地估计IFN-α受体的表观分子量，同时也为追踪游离受体在SDS-聚丙烯酰胺凝胶电泳中的迁移提供了一种工具。
