Based on these data, which of the following proteins (biotin, hygromycin, and streptavidin) can rule out its presence? Briefly explain your answer. What protein is most likely defective in the mutant cells and why?
Experiments are performed to analyze protein tyrosine phosphorylation in response to TCR stimulation. For these experiments, T cells are stimulated with anti-CD3 antibody, and then lysates are prepared and run on a protein (SDS-PAGE) gel to separate the proteins by molecular weight. The proteins are transferred from the gel to a membrane for immunoblotting using an antibody that binds to all phosphorylated tyrosine residues in any protein; this antibody is called ‘anti-phospho-tyrosine antibody,’ and is abbreviated as anti-P-Y. The results are shown in the figure below. You confirm that the mutant T cells express normal levels of all the proteins detected in the WT cells, including PLC-g, SLP-76, ITK, ZAP-70, LCK, LAT, and the CD3 and TCRz proteins.
- Based on these data, which of the following proteins (biotin, hygromycin, and streptavidin) can rule out its presence? Briefly explain your answer.
- What protein is most likely defective in the mutant cells and why?
- For the protein you named in your answer to part (c), which amino acids or domain of the protein could be mutated to account for all the data.
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