Sickle cell hemoglobin (HbS) is an example of a genetic variant of human hemoglobin
where a point mutation in the β globin gene results in substitution of glutamic acid to valine …

The primary pathogenic event of sickle cell anemia is the polymerization of the mutant
hemoglobin (Hb) S within the red blood cells, occurring when HbS is in deoxy state in the …

Sickle cell disease is caused by a mutant form of hemoglobin, hemoglobin S, that
polymerizes under hypoxic conditions. The extent and mechanism of polymerization are …

Thermal stabilities of chicken, grey lag goose (Anser anser), turkey as avian hemoglobins
(Hbs); and human, bovine, sheep and horse as mammalian Hbs in hemolysate form were …

The pathophysiology of sickle cell disease (SCD) is dependent on the polymerization of
deoxygenated sickle hemoglobin (HbS), leading to erythrocyte deformation (sickling) and …

Recent studies have suggested that nitric oxide (NO) binding to hemoglobin (Hb) may lead
to the inhibition of sickle cell fiber formation and the dissolution of sickle cell fibers. NO can …

The structure of sickle cell hemoglobin (Hb S)(β6 Glu→ Val) fibers was probed using UV
resonance Raman (UVRR) spectroscopy. For these studies a functional analogue of Hb S …

Hemopexin (Hx) was isolated from pig blood using hemin-agarose chromatography. The
effect of addition of Hx on hemin and hemoglobin (Hb) mediated lipid oxidation in washed …

In sickle cell hemoglobin, individual tetramers associate into long fibers as a consequence
of the mutation at the β6 position. In this study UV resonance Raman spectroscopy is used to …

In sickle cell anemia, polymerization of hemoglobin in its deoxy state leads to the formation
of insoluble fibers that result in sickling of red blood cells. Stereo-specific binding of …