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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Main Authors: CONDO', SAVERIO GIOVANNI, el Sherbini, S, Giardina, B.
Other Authors: Condo', Sg, Giardina, B
Format: Article in Journal/Newspaper
Language:English
Published: 1991
Subjects:
Online Access:http://hdl.handle.net/2108/54789
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spelling 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
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