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Titolo:
Adult and fetal haemoglobin J-Sardegna [alpha 50(CE8)His -> Asp]: functional and molecular modelling studies
Autore:
Corda, M; De Rosa, WC; Pellegrini, MG; Sanna, MT; Olianas, A; Fais, A; Manca, L; Masala, B; Zappacosta, B; Ficarra, S; Castagnola, M; Giardina, B;
Indirizzi:
Catholic Univ Sacred Heart, Inst Chem & Clin Chem, CNR, Receptor Chem Ctr Rome, I-00168 Rome, Italy Catholic Univ Sacred Heart Rome Italy I-00168 Rome, I-00168 Rome, Italy Univ Cagliari, Dept Biochem & Human Physiol, I-09042 Monserrato Cagliari, Italy Univ Cagliari Monserrato Cagliari Italy I-09042 nserrato Cagliari, Italy Univ Sassari, Dept Physiol & Biochem Sci, I-07100 Sassari, Italy Univ Sassari Sassari Italy I-07100 & Biochem Sci, I-07100 Sassari, Italy Univ Messina, Dept Organ & Biol Chem, I-98010 Messina, Italy Univ MessinaMessina Italy I-98010 n & Biol Chem, I-98010 Messina, Italy
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 346, anno: 2000,
parte:, 1
pagine: 193 - 199
SICI:
0264-6021(20000215)346:<193:AAFHJ[>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
OXYGEN-BINDING; HEMOGLOBIN;
Keywords:
Hb variants; alpha(1)beta(1)interface; molecular dynamics; oxygen affinity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Giardina, B Catholic Univ Sacred Heart, Inst Chem & Clin Chem, CNR, Receptor Chem Ctr Rome, Lgo F Vito 1, I-00168 Rome, Italy Catholic Univ Sacred Heart Lgo F Vito 1 Rome Italy I-00168 ly
Citazione:
M. Corda et al., "Adult and fetal haemoglobin J-Sardegna [alpha 50(CE8)His -> Asp]: functional and molecular modelling studies", BIOCHEM J, 346, 2000, pp. 193-199

Abstract

Haemoglobin (Hb) J-Sardegna [alpha 50(CE8)His --> Asp] is a haemoglobin variant characteristic of subjects from the island of Sardinia, Here we report a study of the functional properties of both fetal and adult Hb J-Sardegna. The results indicate that adult Hb J-Sardegna displays an oxygen affinity that is higher than that of adult Hb only in the presence of 2,3-diphosphoglycerate (2,3-DPG), On the contrary, at 20 degrees C, the oxygen affinityof fetal Hb J-Sardegna is identical to that of normal fetal haemoglobin, both in the presence and in the absence of 2,3-DPG. A significant differencebetween these two systems (i.e. a higher oxygen affinity of fetal Hb J-Sardegna) shows up very clearly only when temperature is increased to 37 degrees C. Hence in fetal Hb, the main effect of the amino acid substitution is a decrease in the overall enthalpy change of oxygenation. The results outline the role of the alpha(1)-beta(1) interface in assessing the thermodynamics of oxygen binding. The functional properties of both adult and fetal Hb J-Sardegna have been interpreted at the structural level in light of the results obtained by a computational modelling approach performed in comparison with HbA and Hb Aichi, a variant characterized by a different mutation [alpha 50(CE8)His --> Arg] at the same position.

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Documento generato il 03/04/20 alle ore 18:55:57