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The values of K m, V max and k cat of TyrBm in the presence of HQ as a substrate were determined with the following conditions: 50 mM PBS buffer pH 7.4, 0.01 mM CuSO 4 , 6 g ml 1 of purified enzyme, various concentrations of HQ (0.12.0 mM) in the presence of saturating concentration of hydrogen peroxide (100 mM) 51
111 In is linked to octreotide using diethylenetriamine pentaacetic acid, while 90 Y and 177 Lu (Lutathera) are linked using tetraazacyclododecane tetraacetic acid as a chelator 68
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The copper-binding property is not incidental
Glutathione has a genuine and well-characterized role in phase II metabolism
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