Fast changes in environmental oxygen availability translate into shifts in mitochondrial free
radical production. An increase in intraerythrocytic reduced glutathione (GSH) during …

Significance: The broad classes of O2-binding proteins known as hemoglobins (Hbs) carry
out oxygenation and redox functions that allow organisms with significantly different …

Hemoglobin is considered a potentially toxic molecule when released from erythrocytes
during hemolysis, inflammation, or tissue injury. The mechanisms of toxicity involve reduced …

Red blood cells (RBCs) are susceptible to sustained free radical damage during circulation,
while the changes of antioxidant capacity and regulatory mechanism of RBCs under …

Cell-free hemoglobin (Hb) enhances the oxidation-related toxicity associated with
inflammation, ischemia, and hemolytic disorders. Hb is highly vulnerable to oxidative …

Hemoglobin (Hb) released into the circulation during hemolysis and chemically modified Hb
proposed for use as oxygen therapeutics exert toxic effects that are partially attributable to …

The β93 cysteine (β93Cys) residue of hemoglobin is conserved in vertebrates but its
function in the red blood cell (RBC) remains unclear. Because this residue is present at …

BACKGROUND Routine storage of red blood cells (RBCs) results in the progressive
accumulation of storage lesions. While the clinical relevance of these lesions is still a matter …

House mice (genus Mus) harbor extensive allelic variation at two tandemly duplicated genes
that encode the β-chain subunits of adult hemoglobin (Hb). Alternative haplotypes differ in …

The classical role of hemoglobin in the erythrocytes is to carry oxygen from the lungs to the
tissues via the circulation. However, hemoglobin also acts as a redox regulator and as a …