Interaction of hemoglobin with chloride and 2,3‐bisphosphoglycerate
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 [G...
Published in: | European Journal of Biochemistry |
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1990
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crwiley:10.1111/j.1432-1033.1990.tb19427.x 2024-06-02T08:10:29+00:00 Interaction of hemoglobin with chloride and 2,3‐bisphosphoglycerate A comparative approach GIARDINA, Bruno BRIX, Ole COLOSIMO, Alfredo PETRUZZELLI, Raffaele CERRONI, Loredana CONDO, Saverio G. 1990 http://dx.doi.org/10.1111/j.1432-1033.1990.tb19427.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1990.tb19427.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1990.tb19427.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Biochemistry volume 194, issue 1, page 61-65 ISSN 0014-2956 1432-1033 journal-article 1990 crwiley https://doi.org/10.1111/j.1432-1033.1990.tb19427.x 2024-05-03T10:55:51Z 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) P 2 ]. The results obtained with hemoglobins from reindeer and musk ox indicate that their low oxygen affinity and their insensitivity to Gri(2,3) P 2 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) P 2 interactions. In other words, insensitivity of reindeer and musk ox hemoglobins to Gri(2,3) P 2 is mainly due to a decreased affinity constant for this cofactor and to an increased affinity constant for chloride anions; this renders more effective the competition of chloride for the anion‐binding site. On the other hand bat hemoglobin behaves in a completely different way and could be regarded as a type case of low‐affinity hemoglobin since its functional properties are modulated neither by chloride nor by Gri(2,3) P 2 . The results are discussed in the light of the amino acid residues which are known to be involved in the binding of organic phosphates. Article in Journal/Newspaper musk ox Rangifer tarandus Wiley Online Library European Journal of Biochemistry 194 1 61 65 |
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Wiley Online Library |
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English |
description |
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) P 2 ]. The results obtained with hemoglobins from reindeer and musk ox indicate that their low oxygen affinity and their insensitivity to Gri(2,3) P 2 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) P 2 interactions. In other words, insensitivity of reindeer and musk ox hemoglobins to Gri(2,3) P 2 is mainly due to a decreased affinity constant for this cofactor and to an increased affinity constant for chloride anions; this renders more effective the competition of chloride for the anion‐binding site. On the other hand bat hemoglobin behaves in a completely different way and could be regarded as a type case of low‐affinity hemoglobin since its functional properties are modulated neither by chloride nor by Gri(2,3) P 2 . The results are discussed in the light of the amino acid residues which are known to be involved in the binding of organic phosphates. |
format |
Article in Journal/Newspaper |
author |
GIARDINA, Bruno BRIX, Ole COLOSIMO, Alfredo PETRUZZELLI, Raffaele CERRONI, Loredana CONDO, Saverio G. |
spellingShingle |
GIARDINA, Bruno BRIX, Ole COLOSIMO, Alfredo PETRUZZELLI, Raffaele CERRONI, Loredana CONDO, Saverio G. Interaction of hemoglobin with chloride and 2,3‐bisphosphoglycerate |
author_facet |
GIARDINA, Bruno BRIX, Ole COLOSIMO, Alfredo PETRUZZELLI, Raffaele CERRONI, Loredana CONDO, Saverio G. |
author_sort |
GIARDINA, Bruno |
title |
Interaction of hemoglobin with chloride and 2,3‐bisphosphoglycerate |
title_short |
Interaction of hemoglobin with chloride and 2,3‐bisphosphoglycerate |
title_full |
Interaction of hemoglobin with chloride and 2,3‐bisphosphoglycerate |
title_fullStr |
Interaction of hemoglobin with chloride and 2,3‐bisphosphoglycerate |
title_full_unstemmed |
Interaction of hemoglobin with chloride and 2,3‐bisphosphoglycerate |
title_sort |
interaction of hemoglobin with chloride and 2,3‐bisphosphoglycerate |
publisher |
Wiley |
publishDate |
1990 |
url |
http://dx.doi.org/10.1111/j.1432-1033.1990.tb19427.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1990.tb19427.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1990.tb19427.x |
genre |
musk ox Rangifer tarandus |
genre_facet |
musk ox Rangifer tarandus |
op_source |
European Journal of Biochemistry volume 194, issue 1, page 61-65 ISSN 0014-2956 1432-1033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/j.1432-1033.1990.tb19427.x |
container_title |
European Journal of Biochemistry |
container_volume |
194 |
container_issue |
1 |
container_start_page |
61 |
op_container_end_page |
65 |
_version_ |
1800756355062038528 |