| D007501 |
Iron |
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN. |
Iron-56,Iron 56 |
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| D008054 |
Lipid Peroxides |
Peroxides produced in the presence of a free radical by the oxidation of unsaturated fatty acids in the cell in the presence of molecular oxygen. The formation of lipid peroxides results in the destruction of the original lipid leading to the loss of integrity of the membranes. They therefore cause a variety of toxic effects in vivo and their formation is considered a pathological process in biological systems. Their formation can be inhibited by antioxidants, such as vitamin E, structural separation or low oxygen tension. |
Fatty Acid Hydroperoxide,Lipid Peroxide,Lipoperoxide,Fatty Acid Hydroperoxides,Lipid Hydroperoxide,Lipoperoxides,Acid Hydroperoxide, Fatty,Acid Hydroperoxides, Fatty,Hydroperoxide, Fatty Acid,Hydroperoxide, Lipid,Hydroperoxides, Fatty Acid,Peroxide, Lipid,Peroxides, Lipid |
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| D010084 |
Oxidation-Reduction |
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). |
Redox,Oxidation Reduction |
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| D012016 |
Reference Values |
The range or frequency distribution of a measurement in a population (of organisms, organs or things) that has not been selected for the presence of disease or abnormality. |
Normal Range,Normal Values,Reference Ranges,Normal Ranges,Normal Value,Range, Normal,Range, Reference,Ranges, Normal,Ranges, Reference,Reference Range,Reference Value,Value, Normal,Value, Reference,Values, Normal,Values, Reference |
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| D004910 |
Erythrocyte Membrane |
The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS. |
Erythrocyte Ghost,Red Cell Cytoskeleton,Red Cell Ghost,Erythrocyte Cytoskeleton,Cytoskeleton, Erythrocyte,Cytoskeleton, Red Cell,Erythrocyte Cytoskeletons,Erythrocyte Ghosts,Erythrocyte Membranes,Ghost, Erythrocyte,Ghost, Red Cell,Membrane, Erythrocyte,Red Cell Cytoskeletons,Red Cell Ghosts |
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| D006454 |
Hemoglobins |
The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements. |
Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D000755 |
Anemia, Sickle Cell |
A disease characterized by chronic hemolytic anemia, episodic painful crises, and pathologic involvement of many organs. It is the clinical expression of homozygosity for hemoglobin S. |
Hemoglobin S Disease,HbS Disease,Sickle Cell Anemia,Sickle Cell Disease,Sickle Cell Disorders,Sickling Disorder Due to Hemoglobin S,Anemias, Sickle Cell,Cell Disease, Sickle,Cell Diseases, Sickle,Cell Disorder, Sickle,Cell Disorders, Sickle,Disease, Hemoglobin S,Hemoglobin S Diseases,Sickle Cell Anemias,Sickle Cell Diseases,Sickle Cell Disorder |
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| D012805 |
Sickle Cell Trait |
The condition of being heterozygous for hemoglobin S. |
Cell Trait, Sickle,Cell Traits, Sickle,Sickle Cell Traits,Trait, Sickle Cell,Traits, Sickle Cell |
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