US EPA

7494000 

Journal Article 

Interaction of allosteric effectors (ATP, CO2, H+) modulating oxygen affinity of the hemoglobin in the carp, Cyprinus carpio, in vitro 

Wurm, T; Albers, C 

1989 

Yes 

Journal of Comparative Physiology B: Biochemical, Systemic, and Environmental Physiology
ISSN: 0174-1578
EISSN: 1432-136X 

Springer-Verlag 

159 

3 

255-261 

English 

10.1007/BF00691502 

The interaction of allosteric effectors (CO2, ATP, H+) with respect to the oxygen affinity of carp hemoglobin was analyzed by determining oxygen binding curves spectrophotometrically in dilute solutions of stripped hemoglobin at 20°C. The pH range studied was 6.8-8.2. PCO2 was 0, 10 and 70 mmHg (0, 1.33 and 9.3 kPa). ATP/Hb4 was 0, 8 and 24. In the presence of either CO2 or ATP, the effects of the cofactors on P50 were as expected over the whole pH range. In contrast to other published data, each cofactor also had a significant effect on P50 in the presence of the other cofactor. Evidence was obtained that oxylabile carbamate is formed by carp hemoglobin and that the formation of carbamate persists at a lower level in the presence of ATP. The results support the view that the binding of ATP to carp hemoglobin requires only one terminal amino group, leaving the other N-terminal of the β-chain free to react with CO2. © 1989 Springer-Verlag. 

ATP; Carp hemoglobin; CO2; Oxygen affinity; adenosine triphosphate; carbon dioxide; hemoglobin; methemoglobin; animal cell; carp; controlled study; erythrocyte; fish; human cell; methodology; nonhuman; normal human; oxygen affinity; ph