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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Inflammation research 27 (1989), S. 268-270 
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Three distinct N-terminal variants of rhIL-1β can be generated by expression of the IL-1β gene in E. coli; the naturally occurring Ala1 species, Met0-Ala1 and des-Ala1 proteins. Since most studies with rhIL-1β have used a mixture of two or more variants, we have evaluated their individual bioactivities. The variants were resolved by cation exchange HPLC. Bioactivity measurement on murine thymocytes gave a potency order of Ala1 〉 des-Ala1 〉 Met0-IL-1β. Analysis using human T-cells co-stimulated with PMA showed a potency order of Ala1 〉 des-Ala1 〉 Met0-IL-1β. Thus changes in the N-terminal amino acid of IL-1β changes the activity of the protein. Since murine and human T-cells respond similarly, the interactions between the N-terminus of rhIL-1β and their receptors probably occur through comparable mechanisms.
    Type of Medium: Electronic Resource
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