Temperature modulation of bovine hemoglobins
The functional properties of hemoglobin from Egyptian water buffalo have been characterized as a function of pH, temperature and chloride concentration. Alongside overall similarities shared with ox and Arctic ruminant hemoglobins, hemoglobin from buffalo shows significant differences with respect t...
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Language: | English |
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1991
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Online Access: | http://hdl.handle.net/2108/54789 |
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ftunivromatorver:oai:art.torvergata.it:2108/54789 2023-08-20T04:04:19+02:00 Temperature modulation of bovine hemoglobins CONDO', SAVERIO GIOVANNI el Sherbini, S Giardina, B. Condo', Sg el Sherbini, S Giardina, B 1991-06-28 http://hdl.handle.net/2108/54789 eng eng volume:177 issue:3 firstpage:956 lastpage:962 journal:BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS http://hdl.handle.net/2108/54789 Animal Oxyhemoglobin Thermodynamic Human Hydrogen-Ion Concentration Temperature Horse Cattle Hemoglobin Kinetic Buffaloe Deer Species Specificity Settore BIO/10 - BIOCHIMICA info:eu-repo/semantics/article 1991 ftunivromatorver 2023-08-01T23:07:37Z The functional properties of hemoglobin from Egyptian water buffalo have been characterized as a function of pH, temperature and chloride concentration. Alongside overall similarities shared with ox and Arctic ruminant hemoglobins, hemoglobin from buffalo shows significant differences with respect to the effect of temperature. The results obtained may suggest that the limited effect of temperature on oxygen binding recently reported for ox hemoglobin could be regarded as an interesting case of a reminiscence of a past glacial age. Article in Journal/Newspaper Arctic 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 |
Animal Oxyhemoglobin Thermodynamic Human Hydrogen-Ion Concentration Temperature Horse Cattle Hemoglobin Kinetic Buffaloe Deer Species Specificity Settore BIO/10 - BIOCHIMICA |
spellingShingle |
Animal Oxyhemoglobin Thermodynamic Human Hydrogen-Ion Concentration Temperature Horse Cattle Hemoglobin Kinetic Buffaloe Deer Species Specificity Settore BIO/10 - BIOCHIMICA CONDO', SAVERIO GIOVANNI el Sherbini, S Giardina, B. Temperature modulation of bovine hemoglobins |
topic_facet |
Animal Oxyhemoglobin Thermodynamic Human Hydrogen-Ion Concentration Temperature Horse Cattle Hemoglobin Kinetic Buffaloe Deer Species Specificity Settore BIO/10 - BIOCHIMICA |
description |
The functional properties of hemoglobin from Egyptian water buffalo have been characterized as a function of pH, temperature and chloride concentration. Alongside overall similarities shared with ox and Arctic ruminant hemoglobins, hemoglobin from buffalo shows significant differences with respect to the effect of temperature. The results obtained may suggest that the limited effect of temperature on oxygen binding recently reported for ox hemoglobin could be regarded as an interesting case of a reminiscence of a past glacial age. |
author2 |
Condo', Sg el Sherbini, S Giardina, B |
format |
Article in Journal/Newspaper |
author |
CONDO', SAVERIO GIOVANNI el Sherbini, S Giardina, B. |
author_facet |
CONDO', SAVERIO GIOVANNI el Sherbini, S Giardina, B. |
author_sort |
CONDO', SAVERIO GIOVANNI |
title |
Temperature modulation of bovine hemoglobins |
title_short |
Temperature modulation of bovine hemoglobins |
title_full |
Temperature modulation of bovine hemoglobins |
title_fullStr |
Temperature modulation of bovine hemoglobins |
title_full_unstemmed |
Temperature modulation of bovine hemoglobins |
title_sort |
temperature modulation of bovine hemoglobins |
publishDate |
1991 |
url |
http://hdl.handle.net/2108/54789 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_relation |
volume:177 issue:3 firstpage:956 lastpage:962 journal:BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS http://hdl.handle.net/2108/54789 |
_version_ |
1774714709674557440 |