| D010100 |
Oxygen |
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration. |
Dioxygen,Oxygen-16,Oxygen 16 |
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| D004163 |
Diphosphoglyceric Acids |
Glyceric acids where two of the hydroxyl groups have been replaced by phosphates. |
Bisphosphoglycerates,Acids, Diphosphoglyceric |
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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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| D001629 |
Bezafibrate |
An antilipemic agent that lowers CHOLESTEROL and TRIGLYCERIDES. It decreases LOW DENSITY LIPOPROTEINS and increases HIGH DENSITY LIPOPROTEINS. |
Azufibrat,BM-15.075,Befibrat,Beza-Lande,Beza-Puren,Bezabeta,Bezacur,Bezafibrat PB,Bezafisal,Bezalip,Bezamerck,Béfizal,Cedur,Difaterol,Eulitop,Lipox,Reducterol,Regadrin B,Sklerofibrat,Solibay,durabezur,BM 15.075,BM15.075,Beza Lande,Beza Puren |
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| D001665 |
Binding Sites |
The parts of a macromolecule that directly participate in its specific combination with another molecule. |
Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining |
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| D001667 |
Binding, Competitive |
The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements. |
Competitive Binding |
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| D019794 |
2,3-Diphosphoglycerate |
A highly anionic organic phosphate which is present in human red blood cells at about the same molar ratio as hemoglobin. It binds to deoxyhemoglobin but not the oxygenated form, therefore diminishing the oxygen affinity of hemoglobin. This is essential in enabling hemoglobin to unload oxygen in tissue capillaries. It is also an intermediate in the conversion of 3-phosphoglycerate to 2-phosphoglycerate by phosphoglycerate mutase (EC 5.4.2.1). (From Stryer Biochemistry, 4th ed, p160; Enzyme Nomenclature, 1992, p508) |
2,3-Bisphosphoglycerate,2,3-DPG,2,3-Diphosphoglyceric Acid,2,3-Diphosphoglycerate, (D)-Isomer,Glycerate 2,3-Bisphosphate,2,3 Bisphosphoglycerate,2,3 Diphosphoglycerate,2,3 Diphosphoglyceric Acid,2,3-Bisphosphate, Glycerate |
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