Hemoglobin of the lung fish Clarias lazera: isolation and oxygen equilibrium studies |
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| Institution: | 1. Graduate Program in Toxicology, North Carolina State University, Raleigh, NC 27695, United States;2. Department of Biological Sciences, North Carolina State University, Raleigh, NC 27695, United States;3. Center for Human Health and the Environment, North Carolina State University, Raleigh, NC 27695, United States;4. W. M. Keck Center for Behavioral Biology, North Carolina State University, Raleigh, NC 27695, United States |
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| Abstract: | The hemoglobin of the lung fish Clarias lazera has a single component on starch gel electrophoresis. The hemoglobin has a molar mass of c. 68,000 similar to HbA on column chromatography. Clarias hemoglobin has a high oxygen affinity with a low Bohr effect. There is a haem-haem interaction, n, which is pH dependent. The R-state is more stable than the T-state, unlike in most fish hemoglobins. |
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