Oxygen binding of fetal and adult bovine hemoglobin in the presence of organic phosphates and uric acid riboside
| Autor: | R. C. Smith, R. E. Isaacks, G. J. Garbutt, D. R. Harkness |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
P50
Inositol Phosphates Clinical Biochemistry chemistry.chemical_element Oxygen chemistry.chemical_compound Hemoglobins Adenosine Triphosphate Organophosphorus Compounds Oxygen Consumption Pregnancy Fetal hemoglobin Animals Genetics (clinical) Fetal Hemoglobin Fetus Binding Sites Chemistry Biochemistry (medical) Oxygen–haemoglobin dissociation curve Hemoglobin A Hematology Hydrogen-Ion Concentration Diphosphoglyceric Acids Uric Acid Biochemistry Cattle Female Hemoglobin Ribonucleosides Adenosine triphosphate Oxygen binding |
| Zdroj: | Hemoglobin. 3(1) |
| ISSN: | 0363-0269 |
| Popis: | The P50 values of “stripped” fetal and adult bovine hemoglobin were 18.4 and 23.9 respectively. Neither the oxygen-hemoglobin dissociation curve nor the Hill coefficient, n, of fetal or adult bovine hemoglobin was affected by uric acid riboside (UAR), 2,3-diphosphoglyceric acid (2,3-DPG), adenosine triphosphate (ATP), or inositol pentaphosphate (IPP). Combinations of UAR and ATP with adult bovine hemoglobin or 2,3-DPG and ATP with fetal hemoglobin also had no effect. It was concluded that neither adult nor fetal bovine red cells contained an identifiable compound which affects the binding of oxygen to hemoglobin. |
| Databáze: | OpenAIRE |
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