A crystalline synthetic peptide representing the epitope of a monoclonal antibody raised against synthetic interferon-alpha 1 fragment 111-166.

Details

Serval ID
serval:BIB_54DFD62DE4A2
Type
Article: article from journal or magazin.
Collection
Publications
Title
A crystalline synthetic peptide representing the epitope of a monoclonal antibody raised against synthetic interferon-alpha 1 fragment 111-166.
Journal
European Journal of Biochemistry
Author(s)
Aguet M., Salgam P., Gutte B., Arnheiter H.
ISSN
0014-2956 (Print)
ISSN-L
0014-2956
Publication state
Published
Issued date
1985
Volume
146
Number
3
Pages
689-691
Language
english
Abstract
The antigenic determinant recognized by the monoclonal antibody that had been raised against synthetic human interferon-alpha 1 (IFN-alpha 1) fragment 111-166 [Arnheiter, H., Thomas, R.M., Leist, T., Fountoulakis, M., and Gutte, B. (1981) Nature (Lond.) 294, 278-280] and that cross-reacted with human IFN-alpha 1, IFN-alpha 2, and IFN-alpha A made in Escherichia coli, was localized to the region between residues 151 and 166 using synthetic COOH-terminal interferon fragments. In solid-phase radioimmunoassays neither the strongly hydrophilic COOH-terminal nonapeptide IFN 158-166 nor its mixtures with IFN 151-162 or IFN 149-158 showed any measurable interaction with the antigen binding site of the monoclonal antibody. For antibody binding, the full covalent structure of IFN 151-166 was required. Quantitatively very similar results were obtained with IFN 149-166 and IFN 143-166. The synthetic COOH-terminal hexadecapeptide of human IFN-alpha 1 (IFN 151-166) could be crystallized.
Keywords
Antibodies, Monoclonal/immunology, Chromatography, Affinity, Crystallization, Epitopes/analysis, Humans, Interferon Type I/chemical synthesis, Interferon Type I/immunology, Interferon Type I, Recombinant, Peptide Fragments/chemical synthesis, Peptide Fragments/immunology, Radioimmunoassay
Pubmed
Web of science
Open Access
Yes
Create date
28/01/2008 11:36
Last modification date
20/08/2019 14:09
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