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Ia antigens contain two distinct forms of β chain

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Abstract

Two new forms of β chain, β 1 and β 2, in I-A immunoprecipitates are described, which differ in their migration values in SDS-PAGE under nonreducing conditions, but which migrate identically in a reduced form. This behavior is very likely due to a different arrangement of intramolecular disulfide bonds which may influence mobility in SDS-PAGE. Peptide map analysis confirmed that β 1 and β 2, possess identical primary polypeptide structures. These two forms of β chain are also expressed on the cell surface and it is suggested that both associate with α chains. The structural differences in these complexes may lead to an increase in heterogeneity of la antigens which could be of importance for T-cell recognition.

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  1. Institut für Immunologie und Genetik, Deutsches Krebsforschungszentrum, Heidelberg, Germany

    Norbert Koch & Günter J. Hämmerling

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  1. Norbert Koch
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  2. Günter J. Hämmerling
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Koch, N., Hämmerling, G.J. Ia antigens contain two distinct forms of β chain. Immunogenetics 14, 437–444 (1981). https://doi.org/10.1007/BF00373324

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  • DOI: https://doi.org/10.1007/BF00373324

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