The Hemoglobins of the Antarctic Fishes Artedidraco orianae and Pogonophryne scotti AMINO ACID SEQUENCE, LACK OF COOPERATIVITY, AND LIGAND BINDING PROPERTIES
The oxygen-transport system of two species of Antarctic fishes belonging to the family Artedidraconidae,Artedidraco orianae and Pogonophryne scotti, was thoroughly investigated. The complete amino acid sequence of the α and β chains of the single hemoglobins of the two species was established. The o...
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1998
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ftopenaccessrep:oai:zenodo.org:93851 2023-10-25T01:30:54+02:00 The Hemoglobins of the Antarctic Fishes Artedidraco orianae and Pogonophryne scotti AMINO ACID SEQUENCE, LACK OF COOPERATIVITY, AND LIGAND BINDING PROPERTIES Massimo Coletta Mario R. Romano Andreas Kunzmann Maurizio Tamburrini Vito Carratore Guido di Prisco 1998-12-01 https://www.openaccessrepository.it/record/93851 https://doi.org/10.1074/jbc.273.49.32452 eng eng url:https://www.openaccessrepository.it/communities/itmirror https://www.openaccessrepository.it/record/93851 doi:10.1074/jbc.273.49.32452 info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ Cell Biology Molecular Biology Biochemistry info:eu-repo/semantics/article publication-article 1998 ftopenaccessrep https://doi.org/10.1074/jbc.273.49.32452 2023-09-26T22:18:20Z The oxygen-transport system of two species of Antarctic fishes belonging to the family Artedidraconidae,Artedidraco orianae and Pogonophryne scotti, was thoroughly investigated. The complete amino acid sequence of the α and β chains of the single hemoglobins of the two species was established. The oxygen-binding properties were also investigated, and were found not to differ significantly from those shown by blood, intact erythrocytes, and unstripped hemolysates. Both hemoglobins have unusually high oxygen affinity and display a relatively small Bohr effect; the Root effect is elicited only by organophosphates and is also reduced. Remarkably, the Hill coefficient is close to one in the whole pH range, indicating absence of cooperative oxygen binding which, in A. orianae hemoglobin, could be ascribed to the subunit heterogeneity shown upon oxygen dissociation. In comparison with the other families of the suborder Notothenioidei, the oxygen-transport system of these two species of Artedidraconidae has unique characteristics, which raise interesting questions on the mode of function of a multisubunit molecule and the relationship with cold adaptation. Article in Journal/Newspaper Antarc* Antarctic Istituto Nazionale di Fisica Nucleare (INFN): Open Access Repository Antarctic The Antarctic Journal of Biological Chemistry 273 49 32452 32459 |
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Open Polar |
collection |
Istituto Nazionale di Fisica Nucleare (INFN): Open Access Repository |
op_collection_id |
ftopenaccessrep |
language |
English |
topic |
Cell Biology Molecular Biology Biochemistry |
spellingShingle |
Cell Biology Molecular Biology Biochemistry Massimo Coletta Mario R. Romano Andreas Kunzmann Maurizio Tamburrini Vito Carratore Guido di Prisco The Hemoglobins of the Antarctic Fishes Artedidraco orianae and Pogonophryne scotti AMINO ACID SEQUENCE, LACK OF COOPERATIVITY, AND LIGAND BINDING PROPERTIES |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
The oxygen-transport system of two species of Antarctic fishes belonging to the family Artedidraconidae,Artedidraco orianae and Pogonophryne scotti, was thoroughly investigated. The complete amino acid sequence of the α and β chains of the single hemoglobins of the two species was established. The oxygen-binding properties were also investigated, and were found not to differ significantly from those shown by blood, intact erythrocytes, and unstripped hemolysates. Both hemoglobins have unusually high oxygen affinity and display a relatively small Bohr effect; the Root effect is elicited only by organophosphates and is also reduced. Remarkably, the Hill coefficient is close to one in the whole pH range, indicating absence of cooperative oxygen binding which, in A. orianae hemoglobin, could be ascribed to the subunit heterogeneity shown upon oxygen dissociation. In comparison with the other families of the suborder Notothenioidei, the oxygen-transport system of these two species of Artedidraconidae has unique characteristics, which raise interesting questions on the mode of function of a multisubunit molecule and the relationship with cold adaptation. |
format |
Article in Journal/Newspaper |
author |
Massimo Coletta Mario R. Romano Andreas Kunzmann Maurizio Tamburrini Vito Carratore Guido di Prisco |
author_facet |
Massimo Coletta Mario R. Romano Andreas Kunzmann Maurizio Tamburrini Vito Carratore Guido di Prisco |
author_sort |
Massimo Coletta |
title |
The Hemoglobins of the Antarctic Fishes Artedidraco orianae and Pogonophryne scotti AMINO ACID SEQUENCE, LACK OF COOPERATIVITY, AND LIGAND BINDING PROPERTIES |
title_short |
The Hemoglobins of the Antarctic Fishes Artedidraco orianae and Pogonophryne scotti AMINO ACID SEQUENCE, LACK OF COOPERATIVITY, AND LIGAND BINDING PROPERTIES |
title_full |
The Hemoglobins of the Antarctic Fishes Artedidraco orianae and Pogonophryne scotti AMINO ACID SEQUENCE, LACK OF COOPERATIVITY, AND LIGAND BINDING PROPERTIES |
title_fullStr |
The Hemoglobins of the Antarctic Fishes Artedidraco orianae and Pogonophryne scotti AMINO ACID SEQUENCE, LACK OF COOPERATIVITY, AND LIGAND BINDING PROPERTIES |
title_full_unstemmed |
The Hemoglobins of the Antarctic Fishes Artedidraco orianae and Pogonophryne scotti AMINO ACID SEQUENCE, LACK OF COOPERATIVITY, AND LIGAND BINDING PROPERTIES |
title_sort |
hemoglobins of the antarctic fishes artedidraco orianae and pogonophryne scotti amino acid sequence, lack of cooperativity, and ligand binding properties |
publishDate |
1998 |
url |
https://www.openaccessrepository.it/record/93851 https://doi.org/10.1074/jbc.273.49.32452 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
url:https://www.openaccessrepository.it/communities/itmirror https://www.openaccessrepository.it/record/93851 doi:10.1074/jbc.273.49.32452 |
op_rights |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.1074/jbc.273.49.32452 |
container_title |
Journal of Biological Chemistry |
container_volume |
273 |
container_issue |
49 |
container_start_page |
32452 |
op_container_end_page |
32459 |
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1780742559511871488 |