Equilibria and kinetic of oxygen and carbon monoxide binding to the haemoglobin of the South American lungfish,Lepidosiren paradoxa |
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| Affiliation: | 1. Department of Biological Sciences, University of Lancaster, Lancaster LA1 4YQ, England;2. Duke University, Marine Laboratories, Beaufort, NC 28516, U.S.A.;3. Zoological Institute, University of Oslo, Blindern, Oslo 3, Norway;4. Department of Zoology, University of Texas at Austin, Austin, TX 78712, U.S.A.;5. Department of Medicine and Biochemistry, Veterans Administration Hospital, S.U.N.Y., Buffalo, NY 14215, U.S.A.;6. Department of Biology, Johns Hopkins University, Baltimore, MD 21218, U.S.A. |
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| Abstract: | - 1. The haemoglobin of the South American lungfishLepidosiren paradoxa has a single component.
- 2. The equilibria of this respiratory protein with oxygen have been investigated both in the blood and with the purified haemoglobin. There is a substantial, normal, alkaline Bohr effect and marked sensitivity to organic phosphates in the haemoglobin solutions.
- 3. Studies on the pH dependence of the kinetics of oxygen dissociation can be interpreted in terms of a normal Bohr effect.
- 4. The kinetics of combination of carbon monoxide have an unusual pH dependence.
- 5. These findings are discussed in terms of the two-state model of Monodet al. (1965)
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