| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1947735 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2011 | 6 Pages |
Abstract
⺠HbF-Monserrato-Sassari is a newly discovered abnormal human fetal hemoglobin. ⺠It is characterized by the Arg for Cys replacement at position 93 of the Gγ globin. ⺠It shows increased oxygen affinity, slightly decreased Bohr effect and cooperativity. ⺠Cys γ93 has a key role for subunit cooperativity in the T â R transition of the HbF. ⺠Substitutions at this position may stabilize the high affinity R-state of the Hb and endanger nitric oxide transport.
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Biochemistry
![Functional properties of the newly observed Gγ-chain fetal hemoglobin variant Hb F-Monserrato-Sassari (HBG2:c.280T > C) or [Gγ93 (F9) Cys â Arg]](/preview/png/1947735.png "First Page Preview: Functional properties of the newly observed Gγ-chain fetal hemoglobin variant Hb F-Monserrato-Sassari (HBG2:c.280T > C) or [Gγ93 (F9) Cys â Arg]")
Authors
Mariagiuseppina Pellegrini, Barbara Manconi, Alessandra Olianas, Maria Teresa Sanna, Claudia Meloni, Monica Pirastru, Paolo Mereu, Giovanni Leoni, Bruno Masala, Laura Manca,