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Oxidation of low-density lipoprotein by hemoglobin stems from a heme-initiated globin radical: antioxidant role of haptoglobin.
It is concluded that the active species in hemoglobin-induced LDL oxidation is the globin radical, as suggested in the third mechanism, and that haptoglobin functions as a major antioxidant thus protecting the vascular system.
Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore.
The binding of hemoglobin to red cell membranes was found to be reversible and electrostatic in nature.
Haptoglobin phenotypes differ in their ability to inhibit heme transfer from hemoglobin to LDL.
It is concluded that partial heme transfer from the Hb-Hp2-2 complex to LDL is the reason for oxidation of LDL lipids as well as protein, and this findings provide a molecular basis for Hp 2-2 atherogenic properties.
The influence of heme-binding proteins in heme-catalyzed oxidations.
The association of human erythrocyte catalase with the cell membrane.
Mechanism of low-density lipoprotein oxidation by hemoglobin-derived iron.
It is concluded that met-hemoglobin exerts its oxidative activity on LDL via transfer of heme, which serves as a vehicle for iron insertion into the LDL protein, leading to formation of atherogenic LDL aggregates.
Association of hemoglobin C with erythrocyte ghosts.
The membrane binding of Hb C at pH values of 6.8 to 7.0 indicates that this reaction may occur under physiological circumstances, and the cytoplasmic portions of band 3 membrane proteins were suggested to be the binding sites for both hemoglobins.
Classification and localization of hemoglobin binding sites on the red blood cell membrane.
The competition of hemoglobin and glyceraldehyde-3-phosphate dehydrogenase suggests band III proteins as a potential binding site for hemoglobin.