Abstract
The reagent 2,2′-biquinoline in glacial acetic acid has been used by a number of workers to measure cuprous-ion concentration in copper proteins. It is shown that the use of this reagent with Limulus hemocyanin gives incorrect results because of the presence of sulfhydryl groups in the protein which are capable of reducing cupric ion. The addition of three moles of p-mercuribenzoate per mole of copper is just sufficient to prevent this reduction. It is also possible to avoid reduction of cupric ion by modification of the biquinoline reagent with ethylenediaminetetraacetic acid. The modified method is generally applicable to the measurement of protein-bound cuprous ion in the presence of reducing groups or molecules.
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