Murine Ia and human DR antigens: homology of amino-terminal sequences.
AUTOR(ES)
Allison, J P
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=392907Documentos Relacionados
- Activation of human raf transforming genes by deletion of normal amino-terminal coding sequences.
- Differential regulation of NF-kappaB2(p100) processing and control by amino-terminal sequences.
- Large hepatitis delta antigen in packaging and replication inhibition: role of the carboxyl-terminal 19 amino acids and amino-terminal sequences.
- Chromatographic isolation of the hemagglutinin polypeptides from influenza virus vaccine and determination of their amino-terminal sequences.
- Structure of murine Ia antigens: partial NH2-terminal amino acid sequences of products of the I-E or I-C subregion.