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Complex formation of class I transplantation antigens and a viral glycoprotein
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.
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.