The interplay of temperature and protons in the modulation of oxygen binding by squid blood
An extensive set of data relating to the binding of oxygen by haemocyanin from the squid Todarodes sagittatus has been collected under various experimental conditions. The results obtained show that, within the range of physiological pH, the concentration of protons affects mainly the high-affinity...
Main Authors: | , , |
---|---|
Other Authors: | , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
1992
|
Subjects: | |
Online Access: | http://hdl.handle.net/2108/54782 |
id |
ftunivromatorver:oai:art.torvergata.it:2108/54782 |
---|---|
record_format |
openpolar |
spelling |
ftunivromatorver:oai:art.torvergata.it:2108/54782 2023-08-20T04:04:37+02:00 The interplay of temperature and protons in the modulation of oxygen binding by squid blood Giardina, B Brix, O. CONDO', SAVERIO GIOVANNI Giardina, B Condo', Sg Brix, O 1992-02-01 http://hdl.handle.net/2108/54782 eng eng volume:281 ( Pt 3) firstpage:725 lastpage:728 journal:BIOCHEMICAL JOURNAL http://hdl.handle.net/2108/54782 Oxygen Animal Thermodynamic Mammal Proton Hydrogen-Ion Concentration Hemocyanin Temperature Decapodiforme Reindeer Whales Settore BIO/10 - BIOCHIMICA info:eu-repo/semantics/article 1992 ftunivromatorver 2023-08-01T23:09:54Z An extensive set of data relating to the binding of oxygen by haemocyanin from the squid Todarodes sagittatus has been collected under various experimental conditions. The results obtained show that, within the range of physiological pH, the concentration of protons affects mainly the high-affinity state of the molecule without significantly affecting the low-affinity state. As far as the effect of temperature is concerned, the data show a characteristic feature which is very similar to that previously described in the case of haemoglobins from Arctic mammals such as reindeer (Rangifer tarandus) and musk ox. (Ovibos moschatus). The shape of the oxygen equilibrium curve shows strong temperature-dependence, since the overall heat of the binding of oxygen to the low-affinity state of the molecule is strongly exothermic and that to the high-affinity state is very close to zero. The results provide an outline of the intramolecular compromise that, through the interplay of temperature and protons, optimizes the loading and unloading of oxygen under the various environmental conditions experienced by this species of squid. Article in Journal/Newspaper Arctic musk ox ovibos moschatus Rangifer tarandus Universitá degli Studi di Roma "Tor Vergata": ART - Archivio Istituzionale della Ricerca Arctic |
institution |
Open Polar |
collection |
Universitá degli Studi di Roma "Tor Vergata": ART - Archivio Istituzionale della Ricerca |
op_collection_id |
ftunivromatorver |
language |
English |
topic |
Oxygen Animal Thermodynamic Mammal Proton Hydrogen-Ion Concentration Hemocyanin Temperature Decapodiforme Reindeer Whales Settore BIO/10 - BIOCHIMICA |
spellingShingle |
Oxygen Animal Thermodynamic Mammal Proton Hydrogen-Ion Concentration Hemocyanin Temperature Decapodiforme Reindeer Whales Settore BIO/10 - BIOCHIMICA Giardina, B Brix, O. CONDO', SAVERIO GIOVANNI The interplay of temperature and protons in the modulation of oxygen binding by squid blood |
topic_facet |
Oxygen Animal Thermodynamic Mammal Proton Hydrogen-Ion Concentration Hemocyanin Temperature Decapodiforme Reindeer Whales Settore BIO/10 - BIOCHIMICA |
description |
An extensive set of data relating to the binding of oxygen by haemocyanin from the squid Todarodes sagittatus has been collected under various experimental conditions. The results obtained show that, within the range of physiological pH, the concentration of protons affects mainly the high-affinity state of the molecule without significantly affecting the low-affinity state. As far as the effect of temperature is concerned, the data show a characteristic feature which is very similar to that previously described in the case of haemoglobins from Arctic mammals such as reindeer (Rangifer tarandus) and musk ox. (Ovibos moschatus). The shape of the oxygen equilibrium curve shows strong temperature-dependence, since the overall heat of the binding of oxygen to the low-affinity state of the molecule is strongly exothermic and that to the high-affinity state is very close to zero. The results provide an outline of the intramolecular compromise that, through the interplay of temperature and protons, optimizes the loading and unloading of oxygen under the various environmental conditions experienced by this species of squid. |
author2 |
Giardina, B Condo', Sg Brix, O |
format |
Article in Journal/Newspaper |
author |
Giardina, B Brix, O. CONDO', SAVERIO GIOVANNI |
author_facet |
Giardina, B Brix, O. CONDO', SAVERIO GIOVANNI |
author_sort |
Giardina, B |
title |
The interplay of temperature and protons in the modulation of oxygen binding by squid blood |
title_short |
The interplay of temperature and protons in the modulation of oxygen binding by squid blood |
title_full |
The interplay of temperature and protons in the modulation of oxygen binding by squid blood |
title_fullStr |
The interplay of temperature and protons in the modulation of oxygen binding by squid blood |
title_full_unstemmed |
The interplay of temperature and protons in the modulation of oxygen binding by squid blood |
title_sort |
interplay of temperature and protons in the modulation of oxygen binding by squid blood |
publishDate |
1992 |
url |
http://hdl.handle.net/2108/54782 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic musk ox ovibos moschatus Rangifer tarandus |
genre_facet |
Arctic musk ox ovibos moschatus Rangifer tarandus |
op_relation |
volume:281 ( Pt 3) firstpage:725 lastpage:728 journal:BIOCHEMICAL JOURNAL http://hdl.handle.net/2108/54782 |
_version_ |
1774714993012375552 |