| Literature DB >> 2480783 |
N Ida1, S Sakurai, T Hosaka, K Hosoi, T Kunitomo, T Shimazu, T Maruyama, Y Matsuura, M Kohase.
Abstract
Three monoclonal antibodies against human interleukin-6 were established and characterized. One antibody was shown to strongly neutralize both the Ig-inducing and hybridoma/plasmacytoma growth activity of interleukin-6. The results of its epitope analysis using protease treated interleukin-6 and immobilized antibody indicated that this neutralizing antibody binds to a peptide corresponding to Leu151-Lys171 of interleukin-6 molecule. Further analysis using synthetic peptides showed that a shorter peptide corresponding to Ala153-Thr162 can also inhibit the binding of the antibody to interleukin-6. These results suggest that this carboxyl-terminal region plays a crucial role in interleukin-6 functions.Entities:
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Year: 1989 PMID: 2480783 DOI: 10.1016/s0006-291x(89)80027-0
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575