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Titolo:
Different functional modulation by heterotropic ligands (2,3-diphosphoglycerate and chlorides) of the two haemoglobins from fallow-deer (Dama dama)
Autore:
Angeletti, M; Pucciarelli, S; Priori, AM; Canofeni, S; Barra, D; Fioretti, E; Coletta, M;
Indirizzi:
Univ Roma Tor Vergata, Dept Expt Med & Biochem Sci, I-00133 Rome, Italy Univ Roma Tor Vergata Rome Italy I-00133 iochem Sci, I-00133 Rome, Italy Univ Rome La Sapienza, Dept Biochem Sci Alessandro Rossi Fanelli, Rome, Italy Univ Rome La Sapienza Rome Italy Alessandro Rossi Fanelli, Rome, Italy Univ Camerino, Postgrad Sch Biochem & Clin Chem, Dept Mol Cellular & Anim Biol, I-62032 Camerino, Italy Univ Camerino Camerino Italy I-62032 Anim Biol, I-62032 Camerino, Italy
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 3, volume: 268, anno: 2001,
pagine: 603 - 611
SICI:
0014-2956(200102)268:3<603:DFMBHL>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-HEMOGLOBIN; MAMMALIAN HEMOGLOBINS; OXYGEN-AFFINITY; ALLOSTERIC MECHANISM; BOVINE HEMOGLOBIN; SEQUENCE; BINDING; PROTEIN;
Keywords:
haemoglobin; ruminants; primary structure; oxygen binding; heterotropic effectors;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Coletta, M Univ Roma Tor Vergata, Dept Expt Med & Biochem Sci, Via Tor Vergata 135, I-00133 Rome, Italy Univ Roma Tor Vergata Via Tor Vergata 135 Rome Italy I-00133 y
Citazione:
M. Angeletti et al., "Different functional modulation by heterotropic ligands (2,3-diphosphoglycerate and chlorides) of the two haemoglobins from fallow-deer (Dama dama)", EUR J BIOCH, 268(3), 2001, pp. 603-611

Abstract

Two haemoglobin components have been identified and purified from fallow-deer (Dama dama) erythrocytes. They are present in similar amounts and the two tetrameric molecules share the same or chain, while two different beta chains are detected in the two components. The beta chains differ by 14 residues, even though they both have 145 amino-acid residues, which account fora molecular mass of 16 023 and 16 064 Da, respectively, while or chain has141 residues, yielding a molecular mass of 15 142 Da. Compared with human Hb, the N-terminal region of both beta chains shows deletion of Val beta1 and the replacement of His beta2 by a methionyl residue, a modification which is common to most ruminant haemoglobins. Although both isolated components show a low intrinsic affinity for oxygen, meaningfuldifferences between the two haemoglobins have been found with respect to the effect of heterotropic effecters, such as 2,3-diphosphoglycerate and chloride ions. In view of the high sequence homology between the two components, the different effect of heterotropic ligands has been tentatively correlated to possible localized structural variations between beta chains of the two haemoglobin components.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/04/20 alle ore 00:35:03