Your browser doesn't support javascript.
loading
High blood oxygen affinity in the air-breathing swamp eel Monopterus albus.
Damsgaard, Christian; Findorf, Inge; Helbo, Signe; Kocagoz, Yigit; Buchanan, Rasmus; Huong, Do Thi Thanh; Weber, Roy E; Fago, Angela; Bayley, Mark; Wang, Tobias.
Afiliação
  • Damsgaard C; Zoophysiology, Department of Bioscience, Aarhus University, 8000 Aarhus C, Denmark. Electronic address: cdamsg@gmail.com.
  • Findorf I; Zoophysiology, Department of Bioscience, Aarhus University, 8000 Aarhus C, Denmark.
  • Helbo S; Zoophysiology, Department of Bioscience, Aarhus University, 8000 Aarhus C, Denmark.
  • Kocagoz Y; Zoophysiology, Department of Bioscience, Aarhus University, 8000 Aarhus C, Denmark.
  • Buchanan R; Zoophysiology, Department of Bioscience, Aarhus University, 8000 Aarhus C, Denmark.
  • Huong do TT; College of Aquaculture and Fisheries, Can Tho University, Can Tho City, Vietnam.
  • Weber RE; Zoophysiology, Department of Bioscience, Aarhus University, 8000 Aarhus C, Denmark.
  • Fago A; Zoophysiology, Department of Bioscience, Aarhus University, 8000 Aarhus C, Denmark.
  • Bayley M; Zoophysiology, Department of Bioscience, Aarhus University, 8000 Aarhus C, Denmark.
  • Wang T; Zoophysiology, Department of Bioscience, Aarhus University, 8000 Aarhus C, Denmark.
Article em En | MEDLINE | ID: mdl-25139401
The Asian swamp eel (Monopterus albus, Zuiew 1793) is a facultative air-breathing fish with reduced gills. Previous studies have shown that gas exchange seems to occur across the epithelium of the buccopharyngeal cavity, the esophagus and the integument, resulting in substantial diffusion limitations that must be compensated by adaptations in others steps of the O2 transport system to secure adequate O2 delivery to the respiring tissues. We therefore investigated O2 binding properties of whole blood, stripped hemoglobin (Hb), two major isoHb components and the myoglobin (Mb) from M. albus. Whole blood was sampled using indwelling catheters for blood gas analysis and determination of O2 equilibrium curves. Hb was purified to assess the effects of endogenous allosteric effectors, and Mb was isolated from heart and skeletal muscle to determine its O2 binding properties. The blood of M. albus has a high O2 carrying capacity [hematocrit (Hct) of 42.4±4.5%] and binds O2 with an unusually high affinity (P50=2.8±0.4mmHg at 27°C and pH7.7), correlating with insensitivity of the Hb to the anionic allosteric effectors that normally decrease Hb-O2 affinity. In addition, Mb is present at high concentrations in both heart and muscle (5.16±0.99 and 1.08±0.19mg ∙ g wet tissue⁻¹, respectively). We suggest that the high Hct and high blood O2 affinity serve to overcome the low diffusion capacity in the relatively inefficient respiratory surfaces, while high Hct and Mb concentration aid in increasing the O2 flux from the blood to the muscles.
Assuntos
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oxigênio / Consumo de Oxigênio / Hemoglobinas / Smegmamorpha / Proteínas de Peixes / Modelos Biológicos / Mioglobina Limite: Animals País/Região como assunto: Asia Idioma: En Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oxigênio / Consumo de Oxigênio / Hemoglobinas / Smegmamorpha / Proteínas de Peixes / Modelos Biológicos / Mioglobina Limite: Animals País/Região como assunto: Asia Idioma: En Ano de publicação: 2014 Tipo de documento: Article