Thermodynamics of effector binding to hemocyanin : influence of temperature.
Hemocyanins are allosterically regulated oxygen carriers freely dissolved in the blood of many crustaceans. The natural modulator urate accumulates under hypoxic conditions in the hemolymph of Homarus vulgaris, and increases the oxygen affinity of the respiratory pigment. Other non-physiological eff...
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ThinkIR: The University of Louisville's Institutional Repository
2009
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ftunivlouisvir:oai:ir.library.louisville.edu:faculty-1118 2023-05-15T16:08:48+02:00 Thermodynamics of effector binding to hemocyanin : influence of temperature. Pott, Ariane Menze, Michael Grieshaber, Manfred 2009-03-01T08:00:00Z https://ir.library.louisville.edu/faculty/117 https://works.bepress.com/michael_menze/29/download/ unknown ThinkIR: The University of Louisville's Institutional Repository https://ir.library.louisville.edu/faculty/117 https://works.bepress.com/michael_menze/29/download/ Faculty Scholarship Lobster Allosteric model Titration calorimetry Homarus vulgaris Protein interaction Ligand Hemocyanin Biology text 2009 ftunivlouisvir 2023-03-09T16:00:29Z Hemocyanins are allosterically regulated oxygen carriers freely dissolved in the blood of many crustaceans. The natural modulator urate accumulates under hypoxic conditions in the hemolymph of Homarus vulgaris, and increases the oxygen affinity of the respiratory pigment. Other non-physiological effectors such as caffeine, dimethylxanthines and methylxanthines are also known to modulate the oxygen-binding properties of hemocyanin. In order to gain insight into the thermodynamic driving forces of these interactions we analyzed the binding of several urate analogs to dodecameric hemocyanin at different temperatures by employing isothermal titration calorimetry (ITC). All investigated non-physiological effectors including caffeine, dimethylxanthines and methylxanthines bind exothermically to hemocyanin and the binding processes are enthalpy driven. Furthermore, we demonstrated a strong temperature dependent binding of caffeine and dimethylxanthines to the hemocyanin of the European lobster and could show that the binding properties of the effectors to the urate-binding site depend on the hydrophobicity of a given molecule. Text European lobster University of Louisville: ThinkIR |
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University of Louisville: ThinkIR |
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ftunivlouisvir |
language |
unknown |
topic |
Lobster Allosteric model Titration calorimetry Homarus vulgaris Protein interaction Ligand Hemocyanin Biology |
spellingShingle |
Lobster Allosteric model Titration calorimetry Homarus vulgaris Protein interaction Ligand Hemocyanin Biology Pott, Ariane Menze, Michael Grieshaber, Manfred Thermodynamics of effector binding to hemocyanin : influence of temperature. |
topic_facet |
Lobster Allosteric model Titration calorimetry Homarus vulgaris Protein interaction Ligand Hemocyanin Biology |
description |
Hemocyanins are allosterically regulated oxygen carriers freely dissolved in the blood of many crustaceans. The natural modulator urate accumulates under hypoxic conditions in the hemolymph of Homarus vulgaris, and increases the oxygen affinity of the respiratory pigment. Other non-physiological effectors such as caffeine, dimethylxanthines and methylxanthines are also known to modulate the oxygen-binding properties of hemocyanin. In order to gain insight into the thermodynamic driving forces of these interactions we analyzed the binding of several urate analogs to dodecameric hemocyanin at different temperatures by employing isothermal titration calorimetry (ITC). All investigated non-physiological effectors including caffeine, dimethylxanthines and methylxanthines bind exothermically to hemocyanin and the binding processes are enthalpy driven. Furthermore, we demonstrated a strong temperature dependent binding of caffeine and dimethylxanthines to the hemocyanin of the European lobster and could show that the binding properties of the effectors to the urate-binding site depend on the hydrophobicity of a given molecule. |
format |
Text |
author |
Pott, Ariane Menze, Michael Grieshaber, Manfred |
author_facet |
Pott, Ariane Menze, Michael Grieshaber, Manfred |
author_sort |
Pott, Ariane |
title |
Thermodynamics of effector binding to hemocyanin : influence of temperature. |
title_short |
Thermodynamics of effector binding to hemocyanin : influence of temperature. |
title_full |
Thermodynamics of effector binding to hemocyanin : influence of temperature. |
title_fullStr |
Thermodynamics of effector binding to hemocyanin : influence of temperature. |
title_full_unstemmed |
Thermodynamics of effector binding to hemocyanin : influence of temperature. |
title_sort |
thermodynamics of effector binding to hemocyanin : influence of temperature. |
publisher |
ThinkIR: The University of Louisville's Institutional Repository |
publishDate |
2009 |
url |
https://ir.library.louisville.edu/faculty/117 https://works.bepress.com/michael_menze/29/download/ |
genre |
European lobster |
genre_facet |
European lobster |
op_source |
Faculty Scholarship |
op_relation |
https://ir.library.louisville.edu/faculty/117 https://works.bepress.com/michael_menze/29/download/ |
_version_ |
1766404816909631488 |