Molecular adaptation to hibernation: the hemoglobin of Dryomys nitedula

  title={Molecular adaptation to hibernation: the hemoglobin of Dryomys nitedula},
  author={Maria Elisabetta Clementi and Raffaele Petruzzelli and Maria da Graça Filippucci and Concetta Rosa Capo and Francesco Misiti and Bruno Giardina},
  journal={Pfl{\"u}gers Archiv},
Abstract.The oxygen binding properties of Dryomysnitedula hemoglobin (Hb) were investigated as a function of pH both in the absence and in the presence of its physiological cofactors (i.e. chloride ions and 2,3-biphosphoglyceric acid) and at different temperatures. Moreover, the α- and β-chains of the Dryomys Hb were partially sequenced. The results obtained show that the effects of Bohr protons, chloride ions, organic phosphates and temperature are significantly lower for Dryomys Hb than for… 
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Instead of adaptation for improved function in the cold, the key molecular adaptations of hibernation may be to exploit the cold to depress most aspects of biochemical function and then rewarm without damage to restore optimal function of all systems.
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