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Journal of Comparative Physiology B

, Volume 182, Issue 6, pp 821–829 | Cite as

Molecular and physicochemical characterization of hemoglobin from the high-altitude Taiwanese brown-toothed shrew (Episoriculus fumidus)

  • Kevin L. CampbellEmail author
  • Anthony V. Signore
  • Masashi Harada
  • Roy E. Weber
Original Paper

Abstract

Red-toothed shrews (subfamily Soricinae) exhibit the highest mass-specific rates of O2 consumption recorded among eutherian mammals, though surprisingly no data appears to be available on the functional characteristics of their hemoglobin (Hb). As a first step in addressing this shortcoming, we investigated the O2 binding characteristics of Taiwanese brown-toothed shrew (Episoriculus fumidus) Hb and its temperature and pH dependence in the absence and presence of anionic red blood cell effectors. Although comparative data regarding the intrinsic O2 affinity of other shrew species are currently unavailable, our data suggest that the sensitivity of this high-elevation endemic species’ Hb to allosteric effector molecules is similar to that of the two lowland species of white-toothed (crocidurine) shrews examined to date. The efficient exploitation of blood O2 reserves by E. fumidus appears to be achieved via synergistic modulation of O2 affinity by Cl and organic phosphates that moreover dramatically lowers the overall enthalpy of oxygenation of their Hb. Oxygen unloading is presumably further enhanced by a relatively high Bohr effect (ΔLog P 50/ΔpH = −0.69) and marked reduction in the titratable histidine content (predicted low proton buffering value) of the component globin chains relative to human HbA. Notably, however, the limited data available suggest these latter attributes may be widespread among shrews and hence likely are not adaptations to chronic altitudinal hypoxia per se.

Keywords

Shrew Hemoglobin High-altitude Oxygen affinity Enthalpy of oxygenation 

Abbreviations

DPG

2,3-Diphosphoglycerate

Hb

Hemoglobin

IEF

Isoelectric focusing

P50

O2 tension at 50 % Hb–O2 saturation

pKa

Logarithmic acid dissociation constant

n50

Hill’s cooperativity coefficient at half saturation

Tb

Body temperature

pI

Isoelectric point

PO2

Partial pressure of oxygen

ΔH

Enthalpy of oxygenation

Notes

Acknowledgments

Funding from the Natural Sciences and Engineering Research Council (NSERC) of Canada (KLC), the Danish Natural Science Research Council (REW) and the Carlsberg Foundation (REW) are gratefully acknowledged. A.V.S. was supported in part by a NSERC Alexander Graham Bell Canada Graduate Scholarship. We also thank M. Berenbrink for helpful discussions regarding the determination and functional consequences of buffering capacity in mammalian hemoglobins.

Supplementary material

360_2012_659_MOESM1_ESM.doc (40 kb)
Supplementary material 1 (DOC 40 kb)

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Copyright information

© Springer-Verlag 2012

Authors and Affiliations

  • Kevin L. Campbell
    • 1
    Email author
  • Anthony V. Signore
    • 1
  • Masashi Harada
    • 2
  • Roy E. Weber
    • 3
  1. 1.Department of Biological SciencesUniversity of ManitobaWinnipegCanada
  2. 2.Laboratory Animal Center, Graduate School of MedicineOsaka City UniversityOsakaJapan
  3. 3.Zoophysiology, Department of BioscienceUniversity of AarhusAarhusDenmark

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