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早期胎儿抗原在转化小鼠细胞上的表达。

Expression of early fetal antigens on transformed mouse cells.

作者信息

Gooding L R

出版信息

Cancer Res. 1976 Sep;36(9 PT 2):3499-502.

PMID:975110
Abstract

We have used immunoprecipitation of radioactivity from labeled cell membrane preparations to study further the association between the histocompatibility-2 (H-2) peptides and a tumor-associated embryonic antigen (Ag I) on the surface of L-cells. Since earlier studies had shown that Ag I and H-2 co-cap on L-cells, the present study was initiated to test the hypothesis that Ag I presents an altered H-2 peptide expressed on transformed cells. Indeed, sodium dodecyl sulfate-gel electrophoresis of Ag I shows two major peaks at approximately 110,000 and 40,000 daltons, the latter co-migrating with the major H-2 peptide. However, further analysis using sequential immunoprecipitation indicates that the molecules reacting with antisera to H-2 and to Ag I are separate entities, precipitating independently of one another. This has led us to postulate that Ag I and H-2 participate in a unique kind of association in the cell membrane, that is, that the bonds between them which allow them to co-cap may be in the lipid bilayer itself, and that these bonds are distrupted upon solubilization of the membrane.

摘要

我们利用从标记细胞膜制剂中进行放射性免疫沉淀的方法,进一步研究组织相容性-2(H-2)肽与L细胞表面肿瘤相关胚胎抗原(抗原I)之间的关联。由于早期研究表明抗原I和H-2在L细胞上共帽,因此开展本研究以检验抗原I呈现转化细胞上表达的改变的H-2肽这一假说。实际上,抗原I的十二烷基硫酸钠-凝胶电泳显示在约110,000和40,000道尔顿处有两个主要峰,后者与主要的H-2肽共迁移。然而,使用连续免疫沉淀的进一步分析表明,与抗H-2和抗抗原I血清反应的分子是独立的实体,彼此独立沉淀。这使我们推测抗原I和H-2在细胞膜中参与一种独特的关联,也就是说,它们之间允许其共帽的键可能在脂质双层本身,并且这些键在膜溶解时被破坏。

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