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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Main Authors: C. R. JOHNSON, E. FREIRE, ANGELETTI, Mauro, PUCCIARELLI, Stefania
Other Authors: C. R., Johnson, Angeletti, Mauro, Pucciarelli, Stefania, E., Freire
Format: Article in Journal/Newspaper
Language:English
Published: 1996
Subjects:
Online Access:http://hdl.handle.net/11581/105064
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spelling 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
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