Functional studies on the separated hemoglobin components of an air-breathing catfish,Hoplosternum littorale (Hancock) |
| |
| Affiliation: | 1. College of Fisheries and Life Science, Dalian Ocean University, No.52 Heishijiao Street, Shahekou district, 116023, Dalian, Liaoning, People’s Republic of China;1. Department of Animal Sciences, Stellenbosch University, 7602 Stellenbosch, Private Bag X1, Matieland 7602, South Africa;2. Institute of Metabolic Physiology, Heinrich-Heine-Universität, D-40225 Düsseldorf, Germany;3. Branch: Fisheries Management, Department of Agriculture, Forestry and Fisheries, 8012 Roggebaai, South Africa |
| |
| Abstract: | ![]()
- 1. The two hemoglobins, Hb I and II, of the obligate air-breathing catfish,Hoplosternum littorale have been isolated.
- 2. The unfractionated stripped hemoglobin has a high oxygen affinity, a normal alkaline Bohr effect, and a Root effect.
- 3. Both the Bohr and Root effects are enhanced by 1 mM ATP.
- 4. Stripped Hb I has a relatively high oxygen affinity, a reversed Bohr effect between pH 6.0 and 8.0 (Δlog P502DpH> 0), but no Root effect. Addition of 1 mM ATP to Hb I causes a marked reduction in the oxygen affinity, a change to a normal alkaline Bohr effect (Δlog P50ΔpH< 0), but no Root effect.
- 5. Stripped Hb II has a lower oxygen affinity at low pH and a higher oxygen affinity at high pH than does Hb I. Hb II shows a large alkaline Bohr effect which is only slightly increased by 1 mM ATP and a Root effect at low pH which is enhanced by 1 mM ATP.
- 6. The observed rates of O2 dissociation and of CO combination with Hbs I and II show differences which parallel those observed in the oxygen equilibrium measurements.
|
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
