A simple peroxide-free chemiluminescent assay for hemoglobin

摘要

Hemoglobin constitutes almost 90% of the dry weight of mature erythrocytes and is responsible for the transport of oxygen and carbon dioxide between the lungs and body tissue. The hemebound iron must be in the ferrous oxidation state (Fe(II)), for hemoglobin to bind oxygen reversibly. Oxyhemoglobin can undergo autooxidation to methemoglobin (HbFe(III)) and higher oxidation states in the presence of other oxidants. In vivo, the methemoglobin concentration is less than 1.5% that of ferrous hemoglobin. Sometimes the intracellular mechanisms (e.g., cytochrome b5 methemoglobin reductase, glutathione, or nicotinamide adenine dinucleotide phosphate fl avin reductase) fail to maintain hemoglobin in the ferrous state due to genetic abnormalities,or the presence of toxins or drugs, rendering the hemoglobin nonfunctional. Hemolytic anemia releases hemoglobin from erythrocytes where the free hemoglobin in circulation is subject to oxidative denaturation. Oxidation of hemoglobin has been problematic in the production and storage of hemoglobinbased blood substitutes.