Murine Ia and human DR antigens: homology of amino-terminal sequences. | Zendy

James P. Allison | Zendy; L E Walker | Zendy; William A. Russell | Zendy; M. A. Pellegrino | Zendy; Soldano Ferrone | Zendy; R. Reisfeld | Zendy; J. A. Frelinger | Zendy; Jack Silver | Zendy

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Murine Ia and human DR antigens: homology of amino-terminal sequences.

Author(s) -

James P. Allison,

L E Walker,

William A. Russell,

M. A. Pellegrino,

Soldano Ferrone,

R. Reisfeld,

J. A. Frelinger,

Jack Silver

Publication year - 1978

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.75.8.3953

Subject(s) - antigen , polyacrylamide gel electrophoresis , sodium dodecyl sulfate , immunoprecipitation , gel electrophoresis , molecular mass , microbiology and biotechnology , biochemistry , chemistry , amino acid , homology (biology) , chain (unit) , immunoglobulin light chain , peptide sequence , biology , genetics , gene , antibody , enzyme , physics , astronomy

Murine Ia and human DR antigens were isolated and purified by immunoprecipitation and sodium dodecyl sulfate/polyacrylamide gel electrophoresis with allo- and xenoantisera, respectively. The I-A subregion antigen consists of two chains, designated Aalpha and Abeta, with molecular weights of 35,000 and 26,000, respectively. The I-C subregion antigen likewise consists of two chains, designated Calpha and Cbeta, with molecular weights of 32,000 and 29,000, respectively. Under nonreducing conditions, the Cbeta chain migrates appreciably more rapidly on sodium dodecyl sulfate/polyacrylamide gels than the reduced Cbeta chain, reflecting the presence of an intrachain disulfide bond. The human DR antigen is also a two-chain unit and contains DRalpha and DRbeta components with molecular weights of 34,000 and 28,000, respectively. The DRbeta chain migrates more rapidly before reduction than afterward, like the murine Cbeta chain. The DRbeta and Cbeta chains are also strikingly homologous if a single amino acid shift is imposed on one of those chains. Thus, human DR antigens strongly resemble the murine I-C subregion antigens.

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