Whale (Balaenoptera physalus) haemoglobin: primary structure, functional characterisation and computer modelling studies
The functional properties of haemoglobin from the Mediterranean whale Balaenoptera physalus have been studied as functions of heterotropic effector concentration and temperature. Particular attention has been given to the effect of carbon dioxide and lactate since the animal is specialised. for prol...
Published in: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology |
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Online Access: | http://hdl.handle.net/11584/100286 https://doi.org/10.1016/S1096-4959(02)00229-4 |
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ftunicagliariris:oai:iris.unica.it:11584/100286 2024-04-21T07:57:49+00:00 Whale (Balaenoptera physalus) haemoglobin: primary structure, functional characterisation and computer modelling studies Corda M Tamburrini M De Rosa MC Pellegrini M Giardina B di Prisco G. SANNA, MARIA TERESA FAIS, ANTONELLA OLIANAS, ALESSANDRA Corda, M Tamburrini, M De Rosa, Mc Sanna, MARIA TERESA Fais, Antonella Olianas, Alessandra Pellegrini, M Giardina, B di Prisco, G. 2003 http://hdl.handle.net/11584/100286 https://doi.org/10.1016/S1096-4959(02)00229-4 unknown info:eu-repo/semantics/altIdentifier/pmid/12524033 info:eu-repo/semantics/altIdentifier/wos/WOS:000180509800004 volume:134 issue:1 firstpage:53 lastpage:62 numberofpages:10 journal:COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. PART B, BIOCHEMISTRY & MOLECULAR BIOLOGY http://hdl.handle.net/11584/100286 doi:10.1016/S1096-4959(02)00229-4 info:eu-repo/semantics/article 2003 ftunicagliariris https://doi.org/10.1016/S1096-4959(02)00229-4 2024-03-25T16:04:31Z The functional properties of haemoglobin from the Mediterranean whale Balaenoptera physalus have been studied as functions of heterotropic effector concentration and temperature. Particular attention has been given to the effect of carbon dioxide and lactate since the animal is specialised. for prolonged dives often in cold water. The molecular basis of the functional behaviour and in particular of the weak interaction with 2,3-diphosphoglycerate is discussed in the light of the primary structure and of computer modelling. On these bases, it is suggested that the A2 (Pro-->Ala) substitution observed in the 6 chains of whale haemoglobin may be responsible for the displacement of the A helix known to be a key structural feature in haemoglobins that display an altered interaction with 2,3-diphosphoglycerate as compared with human haemoglobin. The functional and structural results, discussed in the light of a previous study on the haemoglobin from the Arctic whale Balaenoptera acutorostrata, give further insights into the regulatory mechanisms of the interactive effects of temperature, carbon dioxide and lactate. (C) 2002 Elsevier Science Inc. All rights reserved. Article in Journal/Newspaper Balaenoptera acutorostrata Balaenoptera physalus Università degli Studi di Cagliari: UNICA IRIS Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 134 1 53 62 |
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Università degli Studi di Cagliari: UNICA IRIS |
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ftunicagliariris |
language |
unknown |
description |
The functional properties of haemoglobin from the Mediterranean whale Balaenoptera physalus have been studied as functions of heterotropic effector concentration and temperature. Particular attention has been given to the effect of carbon dioxide and lactate since the animal is specialised. for prolonged dives often in cold water. The molecular basis of the functional behaviour and in particular of the weak interaction with 2,3-diphosphoglycerate is discussed in the light of the primary structure and of computer modelling. On these bases, it is suggested that the A2 (Pro-->Ala) substitution observed in the 6 chains of whale haemoglobin may be responsible for the displacement of the A helix known to be a key structural feature in haemoglobins that display an altered interaction with 2,3-diphosphoglycerate as compared with human haemoglobin. The functional and structural results, discussed in the light of a previous study on the haemoglobin from the Arctic whale Balaenoptera acutorostrata, give further insights into the regulatory mechanisms of the interactive effects of temperature, carbon dioxide and lactate. (C) 2002 Elsevier Science Inc. All rights reserved. |
author2 |
Corda, M Tamburrini, M De Rosa, Mc Sanna, MARIA TERESA Fais, Antonella Olianas, Alessandra Pellegrini, M Giardina, B di Prisco, G. |
format |
Article in Journal/Newspaper |
author |
Corda M Tamburrini M De Rosa MC Pellegrini M Giardina B di Prisco G. SANNA, MARIA TERESA FAIS, ANTONELLA OLIANAS, ALESSANDRA |
spellingShingle |
Corda M Tamburrini M De Rosa MC Pellegrini M Giardina B di Prisco G. SANNA, MARIA TERESA FAIS, ANTONELLA OLIANAS, ALESSANDRA Whale (Balaenoptera physalus) haemoglobin: primary structure, functional characterisation and computer modelling studies |
author_facet |
Corda M Tamburrini M De Rosa MC Pellegrini M Giardina B di Prisco G. SANNA, MARIA TERESA FAIS, ANTONELLA OLIANAS, ALESSANDRA |
author_sort |
Corda M |
title |
Whale (Balaenoptera physalus) haemoglobin: primary structure, functional characterisation and computer modelling studies |
title_short |
Whale (Balaenoptera physalus) haemoglobin: primary structure, functional characterisation and computer modelling studies |
title_full |
Whale (Balaenoptera physalus) haemoglobin: primary structure, functional characterisation and computer modelling studies |
title_fullStr |
Whale (Balaenoptera physalus) haemoglobin: primary structure, functional characterisation and computer modelling studies |
title_full_unstemmed |
Whale (Balaenoptera physalus) haemoglobin: primary structure, functional characterisation and computer modelling studies |
title_sort |
whale (balaenoptera physalus) haemoglobin: primary structure, functional characterisation and computer modelling studies |
publishDate |
2003 |
url |
http://hdl.handle.net/11584/100286 https://doi.org/10.1016/S1096-4959(02)00229-4 |
genre |
Balaenoptera acutorostrata Balaenoptera physalus |
genre_facet |
Balaenoptera acutorostrata Balaenoptera physalus |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/12524033 info:eu-repo/semantics/altIdentifier/wos/WOS:000180509800004 volume:134 issue:1 firstpage:53 lastpage:62 numberofpages:10 journal:COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. PART B, BIOCHEMISTRY & MOLECULAR BIOLOGY http://hdl.handle.net/11584/100286 doi:10.1016/S1096-4959(02)00229-4 |
op_doi |
https://doi.org/10.1016/S1096-4959(02)00229-4 |
container_title |
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology |
container_volume |
134 |
container_issue |
1 |
container_start_page |
53 |
op_container_end_page |
62 |
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1796939279218245632 |