Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi.
Antarctic fish of the family Nototheniidae usually have a single major hemoglobin (Hb 1), often a second, minor component (Hb 2, about 5% of the total), and traces of another component (Hb C, less than 1%). These are functionally similar Bohr and Root effect hemoglobins. All species of other highly...
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1994
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ftopenaccessrep:oai:zenodo.org:89131 2023-10-25T01:31:58+02:00 Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. L. Camardella Patrizia Polverino de Laureto Maurizio Tamburrini Carla Caruso M. Romano Rossana D'Avino G. di Prisco Vito Carratore Bruno Rutigliano 1994-04-01 https://www.openaccessrepository.it/record/89131 https://doi.org/10.1016/s0021-9258(17)36935-1 eng eng url:https://www.openaccessrepository.it/communities/itmirror https://www.openaccessrepository.it/record/89131 doi:10.1016/s0021-9258(17)36935-1 info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ Cell Biology Molecular Biology Biochemistry info:eu-repo/semantics/article publication-article 1994 ftopenaccessrep https://doi.org/10.1016/s0021-9258(17)36935-1 2023-09-26T22:17:10Z Antarctic fish of the family Nototheniidae usually have a single major hemoglobin (Hb 1), often a second, minor component (Hb 2, about 5% of the total), and traces of another component (Hb C, less than 1%). These are functionally similar Bohr and Root effect hemoglobins. All species of other highly endemic fish families so far investigated also have one single major hemoglobin. The hematological features of the nototheniid Trematomus newnesi are remarkably different. It is the only Antarctic species in which Hb 1 and Hb 2 display only a very weak Bohr effect and no Root effect. Perhaps consequentially, Hb C (the only component showing regulation of oxygen binding by protons and other effectors) is not present in traces but accounts for 20-25% of the total. The primary structure of the three hemoglobins of T. newnesi and of Root effect HbC present in trace amounts in another nototheniid (Pagothenia bernacchii) is discussed in relationship with oxygen binding and in terms of molecular and stereochemical models. The hemoglobin multiplicity, the oxygen binding features of Hb 1 and Hb 2, and the presence of functionally distinct components, thus reveal that the oxygen transport of T. newnesi has unique characteristics. Article in Journal/Newspaper Antarc* Antarctic Istituto Nazionale di Fisica Nucleare (INFN): Open Access Repository Antarctic The Antarctic Journal of Biological Chemistry 269 13 9675 9681 |
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Open Polar |
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Istituto Nazionale di Fisica Nucleare (INFN): Open Access Repository |
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ftopenaccessrep |
language |
English |
topic |
Cell Biology Molecular Biology Biochemistry |
spellingShingle |
Cell Biology Molecular Biology Biochemistry L. Camardella Patrizia Polverino de Laureto Maurizio Tamburrini Carla Caruso M. Romano Rossana D'Avino G. di Prisco Vito Carratore Bruno Rutigliano Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
Antarctic fish of the family Nototheniidae usually have a single major hemoglobin (Hb 1), often a second, minor component (Hb 2, about 5% of the total), and traces of another component (Hb C, less than 1%). These are functionally similar Bohr and Root effect hemoglobins. All species of other highly endemic fish families so far investigated also have one single major hemoglobin. The hematological features of the nototheniid Trematomus newnesi are remarkably different. It is the only Antarctic species in which Hb 1 and Hb 2 display only a very weak Bohr effect and no Root effect. Perhaps consequentially, Hb C (the only component showing regulation of oxygen binding by protons and other effectors) is not present in traces but accounts for 20-25% of the total. The primary structure of the three hemoglobins of T. newnesi and of Root effect HbC present in trace amounts in another nototheniid (Pagothenia bernacchii) is discussed in relationship with oxygen binding and in terms of molecular and stereochemical models. The hemoglobin multiplicity, the oxygen binding features of Hb 1 and Hb 2, and the presence of functionally distinct components, thus reveal that the oxygen transport of T. newnesi has unique characteristics. |
format |
Article in Journal/Newspaper |
author |
L. Camardella Patrizia Polverino de Laureto Maurizio Tamburrini Carla Caruso M. Romano Rossana D'Avino G. di Prisco Vito Carratore Bruno Rutigliano |
author_facet |
L. Camardella Patrizia Polverino de Laureto Maurizio Tamburrini Carla Caruso M. Romano Rossana D'Avino G. di Prisco Vito Carratore Bruno Rutigliano |
author_sort |
L. Camardella |
title |
Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. |
title_short |
Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. |
title_full |
Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. |
title_fullStr |
Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. |
title_full_unstemmed |
Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. |
title_sort |
molecular characterization of the functionally distinct hemoglobins of the antarctic fish trematomus newnesi. |
publishDate |
1994 |
url |
https://www.openaccessrepository.it/record/89131 https://doi.org/10.1016/s0021-9258(17)36935-1 |
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/89131 doi:10.1016/s0021-9258(17)36935-1 |
op_rights |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.1016/s0021-9258(17)36935-1 |
container_title |
Journal of Biological Chemistry |
container_volume |
269 |
container_issue |
13 |
container_start_page |
9675 |
op_container_end_page |
9681 |
_version_ |
1780727516010381312 |