| First Author | Sanna MT | Year | 1994 |
| Journal | J Biol Chem | Volume | 269 |
| Issue | 28 | Pages | 18338-42 |
| PubMed ID | 7518430 | Mgi Jnum | J:322684 |
| Mgi Id | MGI:7260087 | Doi | 10.1016/S0021-9258(17)32312-8 |
| Citation | Sanna MT, et al. (1994) Functional alterations in adult and fetal hemoglobin Sassari Asp-alpha 126(H9)-->His. The role of alpha 1 alpha 2 contact. J Biol Chem 269(28):18338-42 |
| abstractText | The effects of pH, organic phosphates (2,3-diphosphoglycerate), and temperature on the functional properties of both adult and fetal hemoglobin Sassari alpha (Asp-126-->His) have been studied. The functional properties of the adult variant are characterized by the following: (i) an oxygen affinity higher than that of normal HbA in all the experimental conditions used; (ii) a dramatic reduction of homotropic interactions (n50 very close to unity); and (iii) a significant decrease of the effect of 2,3-diphosphoglycerate, which is 35% lower than that observed on HbA. The fetal variant shows an increased oxygen affinity compared with normal HbF and an almost abolished heme-heme interaction. The molecular basis of these functional differences is discussed in terms of the possible role played by the substitution of alpha (Asp-26-->His) on the stability of the R state of the molecule due to a decreased interaction at the level of alpha 1 alpha 2 contact. |
