P18.19 A technique for radioactively labeling proteins is electrophilic radioiodination in which an aromatic substitution of 131I onto a tyrosine residue is performed as follows: R R 131| + 131| OH OH Using the activity of 13I, one can measure protein lifetimes in a variety of biological processes. 131I undergoes beta decay with a half-life of 8.02 days. Initially, a protein labeled with 131I has a specific activity of 1.0 µCi, which corresponds to 37,000 decay events every second. The protein is suspended in aqueous solution and exposed to oxygen for 5 days. After isolating the protein from solution, the protein sample is found to have a specific activity of 1.0 µCi. Is oxygen reacting with the tyrosine residues of the protein, resulting in the loss of 1311?

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P18.19 A technique for radioactively labeling proteins is electrophilic radioiodination in
which an aromatic substitution of 131I onto a tyrosine residue is performed as follows:
R
131| +
131|
OH
OH
Using the activity of 131I, one can measure protein lifetimes in a variety of biological
processes. 131I undergoes beta decay with a half-life of 8.02 days. Initially, a protein
labeled with 1311I has a specific activity of 1.0 µuCi, which corresponds to 37,000 decay
events every second. The protein is suspended in aqueous solution and exposed to
oxygen for 5 days. After isolating the protein from solution, the protein sample is found
to have a specific activity of 1.0 µCi. Is oxygen reacting with the tyrosine residues of the
protein, resulting in the loss of 131I?
Transcribed Image Text:P18.19 A technique for radioactively labeling proteins is electrophilic radioiodination in which an aromatic substitution of 131I onto a tyrosine residue is performed as follows: R 131| + 131| OH OH Using the activity of 131I, one can measure protein lifetimes in a variety of biological processes. 131I undergoes beta decay with a half-life of 8.02 days. Initially, a protein labeled with 1311I has a specific activity of 1.0 µuCi, which corresponds to 37,000 decay events every second. The protein is suspended in aqueous solution and exposed to oxygen for 5 days. After isolating the protein from solution, the protein sample is found to have a specific activity of 1.0 µCi. Is oxygen reacting with the tyrosine residues of the protein, resulting in the loss of 131I?
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