Respiratory properties of blood in the harbor porpoise, Phocoena phocoena

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Standard

Respiratory properties of blood in the harbor porpoise, Phocoena phocoena. / Soegaard, Lisette B; Hansen, Marie N; van Elk, Cornelis; Brahm, Jesper; Jensen, Frank Bo.

I: Journal of Experimental Biology, Bind 215, Nr. Pt 11, 06.2012, s. 1938-43.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Soegaard, LB, Hansen, MN, van Elk, C, Brahm, J & Jensen, FB 2012, 'Respiratory properties of blood in the harbor porpoise, Phocoena phocoena', Journal of Experimental Biology, bind 215, nr. Pt 11, s. 1938-43. https://doi.org/10.1242/jeb.069872

APA

Soegaard, L. B., Hansen, M. N., van Elk, C., Brahm, J., & Jensen, F. B. (2012). Respiratory properties of blood in the harbor porpoise, Phocoena phocoena. Journal of Experimental Biology, 215(Pt 11), 1938-43. https://doi.org/10.1242/jeb.069872

Vancouver

Soegaard LB, Hansen MN, van Elk C, Brahm J, Jensen FB. Respiratory properties of blood in the harbor porpoise, Phocoena phocoena. Journal of Experimental Biology. 2012 jun.;215(Pt 11):1938-43. https://doi.org/10.1242/jeb.069872

Author

Soegaard, Lisette B ; Hansen, Marie N ; van Elk, Cornelis ; Brahm, Jesper ; Jensen, Frank Bo. / Respiratory properties of blood in the harbor porpoise, Phocoena phocoena. I: Journal of Experimental Biology. 2012 ; Bind 215, Nr. Pt 11. s. 1938-43.

Bibtex

@article{d203353708bb41e8be13bbfca7c78202,
title = "Respiratory properties of blood in the harbor porpoise, Phocoena phocoena",
abstract = "Harbor porpoises are active divers that exchange O(2) and CO(2) with the environment during a fast single breath upon surfacing. We investigated blood O(2)-transporting properties, buffer characteristics, Cl(-) transport via the erythrocyte anion exchanger (AE1), circulating nitric oxide metabolites and hemoglobin nitrite reduction in harbor porpoises with the aim to evaluate traits that are adaptive for diving behavior. Blood O(2) affinity was higher in harbor porpoises than in similar sized terrestrial mammals, as supported by our parallel recordings of O(2) equilibria in sheep and pig blood. Further, O(2) affinity tended to increase with increasing body mass. A high O(2) affinity favors O(2) extraction from the lungs, but a normal Bohr effect (¿logP(50)/¿pH=-0.46) gradually lowers O(2) affinity during dives (where CO(2) accumulates) to assist O(2) off-loading to perfused tissues. The true plasma non-bicarbonate buffer value was moderately higher than in terrestrial mammals and increased upon deoxygenation. Plasma bicarbonate was also relatively high, contributing to increase the overall buffer capacity. The apparent Cl(-) permeability of harbor porpoise erythrocytes was similar to the human value at 37°C, showing absence of a comparative increase in the velocity of erythrocyte HCO(-)(3)/Cl(-) exchange to aid CO(2) excretion. The Q(10) for AE1-mediated Cl(-) transport in harbor porpoises was lower than in humans and seemed to match the Q(10) for metabolism (Q(10)˜2). Plasma nitrite, plasma nitrate and hemoglobin-mediated nitrite reduction were elevated compared with mammalian standards, suggesting that increased nitric oxide bioavailability and nitrite-derived nitric oxide could play important roles in diving physiology.",
author = "Soegaard, {Lisette B} and Hansen, {Marie N} and {van Elk}, Cornelis and Jesper Brahm and Jensen, {Frank Bo}",
year = "2012",
month = jun,
doi = "10.1242/jeb.069872",
language = "English",
volume = "215",
pages = "1938--43",
journal = "Journal of Experimental Biology",
issn = "0022-0949",
publisher = "The/Company of Biologists Ltd.",
number = "Pt 11",

}

RIS

TY - JOUR

T1 - Respiratory properties of blood in the harbor porpoise, Phocoena phocoena

AU - Soegaard, Lisette B

AU - Hansen, Marie N

AU - van Elk, Cornelis

AU - Brahm, Jesper

AU - Jensen, Frank Bo

PY - 2012/6

Y1 - 2012/6

N2 - Harbor porpoises are active divers that exchange O(2) and CO(2) with the environment during a fast single breath upon surfacing. We investigated blood O(2)-transporting properties, buffer characteristics, Cl(-) transport via the erythrocyte anion exchanger (AE1), circulating nitric oxide metabolites and hemoglobin nitrite reduction in harbor porpoises with the aim to evaluate traits that are adaptive for diving behavior. Blood O(2) affinity was higher in harbor porpoises than in similar sized terrestrial mammals, as supported by our parallel recordings of O(2) equilibria in sheep and pig blood. Further, O(2) affinity tended to increase with increasing body mass. A high O(2) affinity favors O(2) extraction from the lungs, but a normal Bohr effect (¿logP(50)/¿pH=-0.46) gradually lowers O(2) affinity during dives (where CO(2) accumulates) to assist O(2) off-loading to perfused tissues. The true plasma non-bicarbonate buffer value was moderately higher than in terrestrial mammals and increased upon deoxygenation. Plasma bicarbonate was also relatively high, contributing to increase the overall buffer capacity. The apparent Cl(-) permeability of harbor porpoise erythrocytes was similar to the human value at 37°C, showing absence of a comparative increase in the velocity of erythrocyte HCO(-)(3)/Cl(-) exchange to aid CO(2) excretion. The Q(10) for AE1-mediated Cl(-) transport in harbor porpoises was lower than in humans and seemed to match the Q(10) for metabolism (Q(10)˜2). Plasma nitrite, plasma nitrate and hemoglobin-mediated nitrite reduction were elevated compared with mammalian standards, suggesting that increased nitric oxide bioavailability and nitrite-derived nitric oxide could play important roles in diving physiology.

AB - Harbor porpoises are active divers that exchange O(2) and CO(2) with the environment during a fast single breath upon surfacing. We investigated blood O(2)-transporting properties, buffer characteristics, Cl(-) transport via the erythrocyte anion exchanger (AE1), circulating nitric oxide metabolites and hemoglobin nitrite reduction in harbor porpoises with the aim to evaluate traits that are adaptive for diving behavior. Blood O(2) affinity was higher in harbor porpoises than in similar sized terrestrial mammals, as supported by our parallel recordings of O(2) equilibria in sheep and pig blood. Further, O(2) affinity tended to increase with increasing body mass. A high O(2) affinity favors O(2) extraction from the lungs, but a normal Bohr effect (¿logP(50)/¿pH=-0.46) gradually lowers O(2) affinity during dives (where CO(2) accumulates) to assist O(2) off-loading to perfused tissues. The true plasma non-bicarbonate buffer value was moderately higher than in terrestrial mammals and increased upon deoxygenation. Plasma bicarbonate was also relatively high, contributing to increase the overall buffer capacity. The apparent Cl(-) permeability of harbor porpoise erythrocytes was similar to the human value at 37°C, showing absence of a comparative increase in the velocity of erythrocyte HCO(-)(3)/Cl(-) exchange to aid CO(2) excretion. The Q(10) for AE1-mediated Cl(-) transport in harbor porpoises was lower than in humans and seemed to match the Q(10) for metabolism (Q(10)˜2). Plasma nitrite, plasma nitrate and hemoglobin-mediated nitrite reduction were elevated compared with mammalian standards, suggesting that increased nitric oxide bioavailability and nitrite-derived nitric oxide could play important roles in diving physiology.

U2 - 10.1242/jeb.069872

DO - 10.1242/jeb.069872

M3 - Journal article

C2 - 22573773

VL - 215

SP - 1938

EP - 1943

JO - Journal of Experimental Biology

JF - Journal of Experimental Biology

SN - 0022-0949

IS - Pt 11

ER -

ID: 38325955