Natural and recombinant Escherichia coli-derived interferon-gamma differ in their reactivity with monoclonal antibody
| Autor: | J Le, B Y Rubin, H C Kelker, C Feit, C Nagler, J Vilcek |
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| Rok vydání: | 1984 |
| Předmět: | |
| Zdroj: | The Journal of Immunology. 132:1300-1304 |
| ISSN: | 1550-6606 0022-1767 |
| Popis: | Monoclonal antibody GIF-1 was found to neutralize human natural immune interferon (IFN-gamma), but not Escherichia coli-derived recombinant IFN-gamma. In addition, GIF-1 antibody failed to immunoprecipitate 125I-labeled recombinant IFN-gamma, whereas it precipitated natural IFN-gamma in a concentration-dependent manner. The lack of recognition of recombinant IFN-gamma by antibody GIF-1 may not be due to the absence of the oligosaccharide moiety in the molecules of recombinant IFN-gamma alone, because removal of carbohydrate from natural IFN-gamma by treatment with a mixture of glycosidases did not alter the selective binding of antibody, i.e., deglycosylated and untreated natural IFN-gamma were equally neutralized and immunoprecipitated by GIF-1 antibody. In addition, a minor monomeric component of natural IFN-gamma with the m.w. of 15,500, which apparently lacks carbohydrate, was also recognized by antibody GIF-1. These results suggest that the discriminative recognition of natural and recombinant IFN-gamma by monoclonal antibody GIF-1 may be due to a conformational difference at or near the active regions of natural and recombinant human IFN-gamma molecules. |
| Databáze: | OpenAIRE |
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