The equilibrium oxygen-binding properties of hemoglobins from reindeer (Rangifer tarandus tarandus), musk ox (Ovibos muschatos) and a bat (Rousettus aegyptiacus) have been investigated with special reference to the effect of heterotrophic ligands such as chloride and 2,3-bisphosphoglycerate [Gri(2,3)P2]. The results obtained with hemoglobins from reindeer and musk ox indicate that their low oxygen affinity and their insensitivity to Gri(2,3)P2 are not only an intrinsic property of the molecule, as proposed in the case of ruminant hemoglobins, but also the results of the interplay between chloride and Gri(2,3)P2 interactions.
Interaction of hemoglobin with chloride and 2,3-bisphosphoglycerate. A comparative approach / Giardina, B.; Brix, O.; Colosimo, Alfredo; Petruzzelli, R.; Cerroni, L.; Condo, S. G.. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - STAMPA. - 194:(1990), pp. 61-65. [10.1111/j.1432-1033.1990.tb19427.x]
Interaction of hemoglobin with chloride and 2,3-bisphosphoglycerate. A comparative approach
COLOSIMO, Alfredo;
1990
Abstract
The equilibrium oxygen-binding properties of hemoglobins from reindeer (Rangifer tarandus tarandus), musk ox (Ovibos muschatos) and a bat (Rousettus aegyptiacus) have been investigated with special reference to the effect of heterotrophic ligands such as chloride and 2,3-bisphosphoglycerate [Gri(2,3)P2]. The results obtained with hemoglobins from reindeer and musk ox indicate that their low oxygen affinity and their insensitivity to Gri(2,3)P2 are not only an intrinsic property of the molecule, as proposed in the case of ruminant hemoglobins, but also the results of the interplay between chloride and Gri(2,3)P2 interactions.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
