1975
DOI: 10.1016/0022-2364(75)90229-2
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An EPR study of manganese(II) binding to 5′-ATP, hemoglobin, and hemocyanin

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Cited by 3 publications
(1 citation statement)
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“…In human blood, the majority of Mn 2+ ions are bound to protein, with about 80% bound to hemoglobin in erythrocytes and another 20% to proteins in plasma such as transferrin and globulin. 50,51 To free-up this protein-bound Mn (II) for electrochemical measurements, blood needs to be fully digested to mineralize the proteins to release all the Mn 2+ ions. Conventionally, blood is digested on a hot block in a strong oxidizer (e.g., nitric acid or a mixture of nitric acid and hydrogen peroxide) at elevated temperature, which mineralizes proteins and releases Mn 2+ .…”
Section: Resultsmentioning
confidence: 99%
“…In human blood, the majority of Mn 2+ ions are bound to protein, with about 80% bound to hemoglobin in erythrocytes and another 20% to proteins in plasma such as transferrin and globulin. 50,51 To free-up this protein-bound Mn (II) for electrochemical measurements, blood needs to be fully digested to mineralize the proteins to release all the Mn 2+ ions. Conventionally, blood is digested on a hot block in a strong oxidizer (e.g., nitric acid or a mixture of nitric acid and hydrogen peroxide) at elevated temperature, which mineralizes proteins and releases Mn 2+ .…”
Section: Resultsmentioning
confidence: 99%