OXYGEN BINDING TO FALLOW-DEER (DAMA DAMA ) HEMOGLOBIN: STEPWISE ENTHALPIES AT PH 7.4
High-precision thin-layer gas-solution microcalorimetry has been used to study the oxygen binding properties of fallow-deer (Dama dama) hemoglobin under physiological conditions. This method measures directly the enthalpy of macromolecular ligand binding by changing the ligand activity in a manner a...
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ftuncamerinoiris:oai:pubblicazioni.unicam.it:11581/105064 2024-04-14T08:18:40+00:00 OXYGEN BINDING TO FALLOW-DEER (DAMA DAMA ) HEMOGLOBIN: STEPWISE ENTHALPIES AT PH 7.4 C. R. JOHNSON E. FREIRE ANGELETTI, Mauro PUCCIARELLI, Stefania C. R., Johnson Angeletti, Mauro Pucciarelli, Stefania E., Freire 1996 http://hdl.handle.net/11581/105064 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:A1996UA08200008 volume:59 issue:1-2 firstpage:107 lastpage:117 numberofpages:11 journal:BIOPHYSICAL CHEMISTRY http://hdl.handle.net/11581/105064 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0030012769 info:eu-repo/semantics/article 1996 ftuncamerinoiris 2024-03-21T20:37:07Z High-precision thin-layer gas-solution microcalorimetry has been used to study the oxygen binding properties of fallow-deer (Dama dama) hemoglobin under physiological conditions. This method measures directly the enthalpy of macromolecular ligand binding by changing the ligand activity in a manner analogous to that of the Gill thin-layer optical apparatus ([1], D. Dolman and S. J. Gill, Anal. Biochem., 87 (1978) 127-134). By logarithmically lowering the partial pressure of oxygen we have generated differential heat binding curves of oxygen binding to fallow-deer hemoglobin in phosphate buffer at pH 7.4. In order to enlarge the data field, the temperature dependence of the oxygen affinity was examined by generating binding curves at a number of different temperatures allowing for separation of enthalpy and free energy parameters. This type of experimental analysis makes no assumption of optical linearity between the various heme groups and reveals initially that overall oxygen binding to fallow-deer hemoglobin is less exothermic and of lower affinity than for human hemoglobin A0. In addition, previous optical work on the ancestrally related reindeer hemoglobin (Rangifer tarandus; [2], B. Giardina, O. Brix, M. Nuutinen, S. Sherbini, A. Bardgard, G. Lazzarino and S. Condo, FEBS Lett., 247 (1989) 135) has indicated that the enthalpy associated with its final two oxygen binding steps is minimal. Our calorimetric determination with fallow-deer hemoglobin also reveals this tendency. Presumably, this adaptation would make it easier for these animals to maintain a consistent hemoglobin oxygen saturation level under environmental conditions where the temperature fluctuates. Article in Journal/Newspaper Rangifer tarandus CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) |
institution |
Open Polar |
collection |
CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) |
op_collection_id |
ftuncamerinoiris |
language |
English |
description |
High-precision thin-layer gas-solution microcalorimetry has been used to study the oxygen binding properties of fallow-deer (Dama dama) hemoglobin under physiological conditions. This method measures directly the enthalpy of macromolecular ligand binding by changing the ligand activity in a manner analogous to that of the Gill thin-layer optical apparatus ([1], D. Dolman and S. J. Gill, Anal. Biochem., 87 (1978) 127-134). By logarithmically lowering the partial pressure of oxygen we have generated differential heat binding curves of oxygen binding to fallow-deer hemoglobin in phosphate buffer at pH 7.4. In order to enlarge the data field, the temperature dependence of the oxygen affinity was examined by generating binding curves at a number of different temperatures allowing for separation of enthalpy and free energy parameters. This type of experimental analysis makes no assumption of optical linearity between the various heme groups and reveals initially that overall oxygen binding to fallow-deer hemoglobin is less exothermic and of lower affinity than for human hemoglobin A0. In addition, previous optical work on the ancestrally related reindeer hemoglobin (Rangifer tarandus; [2], B. Giardina, O. Brix, M. Nuutinen, S. Sherbini, A. Bardgard, G. Lazzarino and S. Condo, FEBS Lett., 247 (1989) 135) has indicated that the enthalpy associated with its final two oxygen binding steps is minimal. Our calorimetric determination with fallow-deer hemoglobin also reveals this tendency. Presumably, this adaptation would make it easier for these animals to maintain a consistent hemoglobin oxygen saturation level under environmental conditions where the temperature fluctuates. |
author2 |
C. R., Johnson Angeletti, Mauro Pucciarelli, Stefania E., Freire |
format |
Article in Journal/Newspaper |
author |
C. R. JOHNSON E. FREIRE ANGELETTI, Mauro PUCCIARELLI, Stefania |
spellingShingle |
C. R. JOHNSON E. FREIRE ANGELETTI, Mauro PUCCIARELLI, Stefania OXYGEN BINDING TO FALLOW-DEER (DAMA DAMA ) HEMOGLOBIN: STEPWISE ENTHALPIES AT PH 7.4 |
author_facet |
C. R. JOHNSON E. FREIRE ANGELETTI, Mauro PUCCIARELLI, Stefania |
author_sort |
C. R. JOHNSON |
title |
OXYGEN BINDING TO FALLOW-DEER (DAMA DAMA ) HEMOGLOBIN: STEPWISE ENTHALPIES AT PH 7.4 |
title_short |
OXYGEN BINDING TO FALLOW-DEER (DAMA DAMA ) HEMOGLOBIN: STEPWISE ENTHALPIES AT PH 7.4 |
title_full |
OXYGEN BINDING TO FALLOW-DEER (DAMA DAMA ) HEMOGLOBIN: STEPWISE ENTHALPIES AT PH 7.4 |
title_fullStr |
OXYGEN BINDING TO FALLOW-DEER (DAMA DAMA ) HEMOGLOBIN: STEPWISE ENTHALPIES AT PH 7.4 |
title_full_unstemmed |
OXYGEN BINDING TO FALLOW-DEER (DAMA DAMA ) HEMOGLOBIN: STEPWISE ENTHALPIES AT PH 7.4 |
title_sort |
oxygen binding to fallow-deer (dama dama ) hemoglobin: stepwise enthalpies at ph 7.4 |
publishDate |
1996 |
url |
http://hdl.handle.net/11581/105064 |
genre |
Rangifer tarandus |
genre_facet |
Rangifer tarandus |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:A1996UA08200008 volume:59 issue:1-2 firstpage:107 lastpage:117 numberofpages:11 journal:BIOPHYSICAL CHEMISTRY http://hdl.handle.net/11581/105064 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0030012769 |
_version_ |
1796318204683878400 |