The Unique Hemoglobin System of Pleuragramma antarcticum, an Antarctic Migratory Teleost STRUCTURE AND FUNCTION OF THE THREE COMPONENTS
Pleuragramma antarcticum (suborder Notothenioidei, family Nototheniidae) is the most abundant fish in the antarctic shelf. This pelagic species has a circum-antarctic distribution and is characterized by spawning migration. This species displays the highest multiplicity of major hemoglobins (three);...
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1996
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ftopenaccessrep:oai:zenodo.org:93487 2023-10-25T01:31:33+02:00 The Unique Hemoglobin System of Pleuragramma antarcticum, an Antarctic Migratory Teleost STRUCTURE AND FUNCTION OF THE THREE COMPONENTS Angela Fago Andreas Kunzmann Guido di Prisco Maurizio Tamburrini Rossana D'Avino Vito Carratore 1996-09-01 https://www.openaccessrepository.it/record/93487 https://doi.org/10.1074/jbc.271.39.23780 eng eng url:https://www.openaccessrepository.it/communities/itmirror https://www.openaccessrepository.it/record/93487 doi:10.1074/jbc.271.39.23780 info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ Cell Biology Molecular Biology Biochemistry info:eu-repo/semantics/article publication-article 1996 ftopenaccessrep https://doi.org/10.1074/jbc.271.39.23780 2023-09-26T22:19:22Z Pleuragramma antarcticum (suborder Notothenioidei, family Nototheniidae) is the most abundant fish in the antarctic shelf. This pelagic species has a circum-antarctic distribution and is characterized by spawning migration. This species displays the highest multiplicity of major hemoglobins (three); the other notothenioids have a single one (except one species, having two) with relatively low oxygen affinity regulated by pH and organophosphates. The hemoglobins of P. antarcticum display strong Bohr and Root effects; however, they reveal important functional differences in subunit cooperativity and organophosphate regulation and, above all, in the response of oxygenation to temperature. Despite the substitution ValbetaE11 --> Ile found in Hb 2, which decreases the affinity in human mutants, the hemoglobins have similar oxygen affinity, higher than that of the other notothenioids. Hb 1 has the alpha chain in common with Hb 2 and the beta in common with Hb 3. The amino acid sequence of all four chains has been established. Thus the hematological features of P. antarcticum differ remarkably from those of antarctic notothenioids. This unique and sophisticated oxygen transport system may adequately meet the requirements of the unusual mode of life of this fish. Article in Journal/Newspaper Antarc* Antarctic Istituto Nazionale di Fisica Nucleare (INFN): Open Access Repository Antarctic The Antarctic Journal of Biological Chemistry 271 39 23780 23785 |
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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 Angela Fago Andreas Kunzmann Guido di Prisco Maurizio Tamburrini Rossana D'Avino Vito Carratore The Unique Hemoglobin System of Pleuragramma antarcticum, an Antarctic Migratory Teleost STRUCTURE AND FUNCTION OF THE THREE COMPONENTS |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
Pleuragramma antarcticum (suborder Notothenioidei, family Nototheniidae) is the most abundant fish in the antarctic shelf. This pelagic species has a circum-antarctic distribution and is characterized by spawning migration. This species displays the highest multiplicity of major hemoglobins (three); the other notothenioids have a single one (except one species, having two) with relatively low oxygen affinity regulated by pH and organophosphates. The hemoglobins of P. antarcticum display strong Bohr and Root effects; however, they reveal important functional differences in subunit cooperativity and organophosphate regulation and, above all, in the response of oxygenation to temperature. Despite the substitution ValbetaE11 --> Ile found in Hb 2, which decreases the affinity in human mutants, the hemoglobins have similar oxygen affinity, higher than that of the other notothenioids. Hb 1 has the alpha chain in common with Hb 2 and the beta in common with Hb 3. The amino acid sequence of all four chains has been established. Thus the hematological features of P. antarcticum differ remarkably from those of antarctic notothenioids. This unique and sophisticated oxygen transport system may adequately meet the requirements of the unusual mode of life of this fish. |
format |
Article in Journal/Newspaper |
author |
Angela Fago Andreas Kunzmann Guido di Prisco Maurizio Tamburrini Rossana D'Avino Vito Carratore |
author_facet |
Angela Fago Andreas Kunzmann Guido di Prisco Maurizio Tamburrini Rossana D'Avino Vito Carratore |
author_sort |
Angela Fago |
title |
The Unique Hemoglobin System of Pleuragramma antarcticum, an Antarctic Migratory Teleost STRUCTURE AND FUNCTION OF THE THREE COMPONENTS |
title_short |
The Unique Hemoglobin System of Pleuragramma antarcticum, an Antarctic Migratory Teleost STRUCTURE AND FUNCTION OF THE THREE COMPONENTS |
title_full |
The Unique Hemoglobin System of Pleuragramma antarcticum, an Antarctic Migratory Teleost STRUCTURE AND FUNCTION OF THE THREE COMPONENTS |
title_fullStr |
The Unique Hemoglobin System of Pleuragramma antarcticum, an Antarctic Migratory Teleost STRUCTURE AND FUNCTION OF THE THREE COMPONENTS |
title_full_unstemmed |
The Unique Hemoglobin System of Pleuragramma antarcticum, an Antarctic Migratory Teleost STRUCTURE AND FUNCTION OF THE THREE COMPONENTS |
title_sort |
unique hemoglobin system of pleuragramma antarcticum, an antarctic migratory teleost structure and function of the three components |
publishDate |
1996 |
url |
https://www.openaccessrepository.it/record/93487 https://doi.org/10.1074/jbc.271.39.23780 |
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/93487 doi:10.1074/jbc.271.39.23780 |
op_rights |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.1074/jbc.271.39.23780 |
container_title |
Journal of Biological Chemistry |
container_volume |
271 |
container_issue |
39 |
container_start_page |
23780 |
op_container_end_page |
23785 |
_version_ |
1780727047274889216 |