Interaction of hemoglobin with chloride and 2,3-bisphosphoglycerate. A comparative approach
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...
Published in: | European Journal of Biochemistry |
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Main Authors: | , , , , , |
Other Authors: | , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Blackwell
1990
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Subjects: | |
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 |
Summary: | 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. |
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