Interaction of hemoglobin with chloride and 2,3-bisphosphoglycerate. A comparative approach

• Published in: European Journal of Biochemistry
• Main Authors: Giardina B., Brix O., Petruzzelli R., Cerroni L., Condo S. G., COLOSIMO, Alfredo
• Other Authors: Giardina, B., Brix, O., Colosimo, Alfredo, Petruzzelli, R., Cerroni, L., Condo, S. G.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Blackwell 1990
• Subjects: hemoglobin; 2 3-bisphosphoglycerate; oxygen binding; musk ox; Rangifer tarandus
• Online Access: http://hdl.handle.net/11573/472946; https://doi.org/10.1111/j.1432-1033.1990.tb19427.x; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=A1990EM19800009&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a; http://www.scopus.com/inward/record.url?eid=2-s2.0-0025250645&partnerID=65&md5=6a8503211ec3f7fef83e57f35aa99d96

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.