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Titolo:
Low-temperature sensitivity and enhanced Bohr effect in red deer (Cervus elaphus) haemoglobin: a molecular adaptive strategy to life at high altitudeand low temperature
Autore:
Pellegrini, M; Giardina, B; Castagnola, M; Olianas, A; Sanna, MT; Fais, A; Messana, I; Corda, M;
Indirizzi:
Univ Cagliari, Dipartimento Biochim & Fisiol Umana, I-09042 Monserrato, CA, Univ Cagliari Monserrato CA Italy I-09042 Umana, I-09042 Monserrato, CA, CNR, Ist Chim & Chim Clin, Ctr Chim Recettori & Mol Biol Att, Rome, Italy CNR Rome Italy him Clin, Ctr Chim Recettori & Mol Biol Att, Rome, Italy
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 3, volume: 260, anno: 1999,
pagine: 667 - 671
SICI:
0014-2956(199903)260:3<667:LSAEBE>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
OXYGEN-AFFINITY; MAMMALIAN HEMOGLOBINS; BOVINE HEMOGLOBIN; FETAL HEMOGLOBIN; ADAPTATION; CHLORIDE; MODULATION; REINDEER; 2,3-DIPHOSPHOGLYCERATE; MECHANISM;
Keywords:
allosteric regulation; enthalpy of oxygenation; hemoglobin; red deer (Cervus elaphus);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Pellegrini, M Univ Cagliari, Dipartimento Biochim & Fisiol Umana, S Prov Monserrato Sestu Univ Cagliari S Prov Monserrato Sestu Km 0-7 Monserrato CA Italy I-09042
Citazione:
M. Pellegrini et al., "Low-temperature sensitivity and enhanced Bohr effect in red deer (Cervus elaphus) haemoglobin: a molecular adaptive strategy to life at high altitudeand low temperature", EUR J BIOCH, 260(3), 1999, pp. 667-671

Abstract

A study of the functional properties of haemoglobin from red deer (Cervus elaphus) whose habitat varies over a wide range of latitude, was performed. The oxygen-binding properties of the most common haemoglobin phenotype from the species living in Sardinia were examined with particular attention tothe effect of pH, chloride, 2,3-bisphosphoglycerate and temperature. Results indicate that red deer haemoglobin, like all haemoglobins from ruminantsso far examined, is characterized by a low intrinsic oxygen affinity, withchloride being its main physiological modulator in vivo. The functional results and the low temperature sensitivity of the oxygen affinity are discussed in the light of the amino acid sequence of closely related ruminant haemoglobins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/06/20 alle ore 00:01:48