Abstract
Summary
Hemoglobin solutions were prepared from erythrocytes that were laked in the presence of nicotinic acid amide, glucose, and ammonia. The solutions were Seitz-filtered, yielding clear solutions free from cellular debris, and containing sufficient of the enzyme systems of the cell to change the pigment from oxyhemoglobin to reduced hemoglobin with no appreciable accumulation of methemoglobin during the process. The solutions could be stored in the reduced state for protracted periods at elevated temperatures without increase in methemoglobin content.
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