| Autor: |
Giardina, Bruno, Scatena, Roberto, Clementi, Maria E., Cerroni, Loredana, Nuutinen, Matti, Brix, Ole, Sletten, Solve N., Castagnola, Massimo, Condò, Saverio G. |
| Zdroj: |
JMB Online (Journal of Molecular Biology); January 1993, Vol. 229 Issue: 2 p512-516, 5p |
| Abstrakt: |
Human fetal hemoglobin is known to display, at 20°C, a lower affinity than human adult hemoglobin for oxygen when both proteins are in the absence of organic phosphates. The physiologically important reverse situation is achieved at 37°C upon addition of 2,3-bisphosphoglycerate (DPG), whose lower effect on fetal hemoglobin is related to some amino acid substitutions present in γ-chains. However, the difference in oxygen affinity observed at 37°C is not solely due to the different modulation power of DPG with respect to adult and fetal hemoglobins. In fact, the results presented here reveal new aspects linked to the interplay of temperature and organic phosphates. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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