hepes has been researched along with 2,3-diphosphoglycerate in 2 studies
*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) [MeSH]
*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) [MeSH]
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (50.00) | 18.7374 |
| 1990's | 1 (50.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Guy, GR; Hawkins, PT; King, CE; Michell, RH; Stephens, LR | 1 |
| Ho, C; Ho, NT; Shen, TJ; Tsai, CH | 1 |
2 other study(ies) available for hepes and 2,3-diphosphoglycerate
| Article | Year |
|---|---|
Multiple metabolic pools of phosphoinositides and phosphatidate in human erythrocytes incubated in a medium that permits rapid transmembrane exchange of phosphate.
Topics: 2,3-Diphosphoglycerate; Adenosine Triphosphate; Calcium; Diphosphoglyceric Acids; Erythrocyte Membrane; Ethers; HEPES; Humans; In Vitro Techniques; Ionomycin; Lipids; Phosphates; Phosphatidic Acids; Phosphatidylinositols; Phosphoric Diester Hydrolases | 1987 |
Effects of substitutions of lysine and aspartic acid for asparagine at beta 108 and of tryptophan for valine at alpha 96 on the structural and functional properties of human normal adult hemoglobin: roles of alpha 1 beta 1 and alpha 1 beta 2 subunit inter
Topics: 2,3-Diphosphoglycerate; Adult; Amino Acid Substitution; Asparagine; Aspartic Acid; Buffers; Chlorides; Hemoglobin A; Hemoglobins; Hemoglobins, Abnormal; HEPES; Humans; Lysine; Nuclear Magnetic Resonance, Biomolecular; Oxygen; Oxyhemoglobins; Phosphates; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Structure-Activity Relationship; Tryptophan; Valine | 1999 |