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Example of SDS-PAGE of proteins visualized by autoradiography. Two radioactively labeled protein samples were run in adjacent lanes of the gel (1, 2). The larger proteins (β-galactosidase size standard, marker, E-cadherin cell-to-cell adhesion protein, pp120) are towards the top of the gel and smaller proteins (vSRC tyrosine-specific protein kinase, 60,000 Da) are towards the bottom. As its name implies, pp120 is a 120,000 Da phosphoprotein. The β-galactosidase and bovine serum albumin (BSA) size standards were in an adjacent lane (not shown). The radioactive label was ³²Phosphate from the gamma position phosphate group of ATP. The vSRC protein is an oncogene that disrupts cell growth by its phosphorylation of other proteins such as β-catenin, a protein that links E-cadherin to the cell's cytoskeleton. In this experiment, the vSRC protein auto-phosphorylated itself and the other proteins (E-cadherin, pp120 and β-catenin). After electrophoresis, medical X-ray film was exposed to the dried gel and regions of dark exposure of the film (the "bands") indicate the position of the radioactively-labeled proteins. Lane 1 is a negative control for which no vSRC was added to the labeling reaction. The other proteins (E-cadherin, pp120 and β-catenin) came from an immunoprecipitation of E-cadherin with anti-E-cadherin antibody. The pp120 and β-catenin proteins exist in a molecular complex with E-cadherin at the surface of the cell and they co-precipitate with E-cadherin. Some cSRC kinase probably also co-precipitated with the E-cadherin, accounting for the faint bands in lane 1. The vSRC kinase was immunoprecipitated from mouse NIH-3T3 cells that had been genetically engineered to express this chicken-derived oncogene. The E-cadherin was from mouse P19 embryonal carcinoma cells. (this picture was worth 290 words)

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