期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1983
卷号：80
期号：5
页码：1445-1448
DOI：10.1073/pnas.80.5.1445
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Immunoprecipitates obtained from [35S]methionine-labeled spleen cells by using monoclonal antibodies specific for H-2Kd and H-2Dd have been separated by two-dimensional polyacrylamide gel electrophoresis. Analysis of these gel patterns revealed the presence of an additional product of the K end of the H-2d complex, designated here as H-2K'. To determine whether H-2K' is a unique protein or a differentially glycosylated form of the previously characterized H-2Kd histocompatibility antigen, nonglycosylated molecules labeled in the presence of tunicamycin were examined. The results showed that both H-2K and H-2K' have distinct nonglycosylated polypeptide precursor forms. The approximate molecular weight differences between the fully glycosylated and nonglycosylated molecules also indicated the presence of three oligosaccharide side chains on H-2K', as is the case with H-2Kd, whereas H-2Dd has only two oligosaccharide units. The cellular expression of H-2K' was also investigated. Comparison of H-2 antigens immunoprecipitated from normal spleen cells and from thioglycollate-induced adherent peritoneal exudate cells cultured in the presence or absence of supernatant fluids from concanavalin A-stimulated spleen cells revealed that H-2K' was not expressed on the adherent peritoneal cells. This indicates that H-2K' is expressed in a tissue-specific manner, unlike the classical histocompatibility antigens H-2K and H-2D.
