The 1 I-kDa E 1 b protein in Ad 12-transformed rat cells and in Ad 12-infected human cells binds lipid strongly. The lipid is not removed by boiling in the presence of SDS or by extraction with methanol/chloroform. It is, however, dissociated from the protein by treatment with methanolic KOH suggesting that attachment is through an ester linkage. The acylated 18-kDa protein is detected only in the membrane fraction. Labelling cell surface proteins on Ad 12-transformed cells with [*ZSI]iodosulphanilic acid shows that some of the Ad 12 18-kDa El b protein is present on the outside of the cell. It is concluded that this protein is responsible for cell surface T-antigen activity.
Adenovirus I2 Ad 12 El protein Tumor antigen Acylation Post-translational modification
Using resistance to the base analog 8-azaguanine as a genetic marker, we showed that adenovirus type 2, but not adenovirus type 12, is mutagenic at the hypoxanthine phosphoribosyltransferase locus of cloned diploid rat liver epithelial cells. Adenovirus type 2 increased the frequency of 8-azaguanine-resistant colonies by up to ninefold over the spontaneous frequency, depending on expression time and virus dose.
A major factor preventing more widespread use of polymerase chain reaction in the clinical laboratory is the lack of convenient non-radioactive probe hybridization procedures which do not sacrifice sensitivity or specificity. In this report, we describe comparisons of probes labelled with biotin, digoxygenin, alkaline phosphatase, and(32)P. We report the comparison of solution or liquid hybridization assay and Southern blotting with digoxygenin-labelled oligonucleotides on a total of 64 clinical specimens. Perfect diagnostic agreement between the(32)P and digoxygenin probes was obtained. These data suggest that the non-radioactive assay as described is as sensitive and as specific as the assay with(32)P-Iabelled probes.
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