Kämpe O, Bellgrau D, Hammerling U, Lind P, Pääbo S, Severinsson L, Peterson P A
J Biol Chem. 1983 Sep 10;258(17):10594-8.
Indirect immunoprecipitations of labeled glycoproteins from the adenovirus-transformed rat cell line A2T2C4 and from adenovirus-infected HeLa cells revealed that the class I major histocompatibility antigens co-precipitated with the viral E19 protein. The degree of co-precipitation was highly dependent on the antiserum used. The identity of the co-precipitated components was verified by peptide mapping and radiochemical amino acid sequencing. Cell-free translation of mRNA for the E19 protein and the class I antigen heavy chains demonstrated that the E19 protein-class I antigen interaction is an inherent property of the participating components. In intact cells the virus protein and the transplantation antigens form large complexes, held together by weak, noncovalent interactions.
对来自腺病毒转化的大鼠细胞系A2T2C4以及腺病毒感染的HeLa细胞的标记糖蛋白进行间接免疫沉淀，结果显示I类主要组织相容性抗原与病毒E19蛋白共沉淀。共沉淀的程度高度依赖于所用的抗血清。通过肽图谱分析和放射化学氨基酸测序验证了共沉淀成分的身份。对E19蛋白和I类抗原重链的mRNA进行无细胞翻译表明，E19蛋白与I类抗原的相互作用是参与成分的固有特性。在完整细胞中，病毒蛋白和移植抗原形成大的复合物，通过弱的非共价相互作用结合在一起。
