X-ray diffraction quality crystals have been obtained from a complex between interferon y and the extracellular domain of its high-affinity cell surface receptor. The crystals were obtained from interferon ylinterferon y receptor complexes purified by size exclusion chromatography. Diffraction quali
Purification of Interferon γ-Interferon γ Receptor Complexes by Preparative Electrophoresis on Native Gels
✍ Scribed by M. Fountoulakis; E. Takacsdilorenzo; J.F. Juranville; M. Manneberg
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 829 KB
- Volume
- 208
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
Cytokine-receptor complexes are required for certain studies including crystallization, NMR spectra, and investigation of the biological response mechanism to the cytokine. The purity of the ligand-receptor complex is critical for most of these applications. We investigated the possibility of purifying protein-protein complexes by electrophoresis on native gels. Starting with partially purified mouse and highly purified human proteins, we prepared milligram amounts of interferon (\gamma)-interferon (\gamma) receptor complexes by preparative electrophoresis on nondenaturing polyacrylamide gels. In both cases, pure ligand-receptor complexes with the correct stoichiometry of binding were recovered. Electrophoresis on preparative native gels may prove to be of general interest for the preparation of protein-protein complexes to be used in diverse studies. (\mathbb{C} 1993) Academic Press, Inc.
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