Human hemoglobin reacted with 2-methoxy-5-nitrotropone at pH 7.4 undergoes modification of the four N-terminal amino groups. The modified protein shows increased oxygen affinity with complete abolition of the effect of K-glycerate 2, 3-bisphosphate. The Bohr effect is abolished in the acid range and drastically reduced at alkaline pH values. Changes in the kinetics of ligand reactions parallel the oxygen equilibrium results. Cooperative effects are still present. Human erythrocytes treated with 2-methoxy-5-nitrotropone show increased oxygen affinity and some decrease in methemoglobin reductase efficiency but no change in resistance to hemolysis.
Currell, D., Benitez, E., Ioppolo, C., Giardina, B., Condo', S.g., Martini, F., et al. (1978). The effect of 2-methoxy-5-nitrotropone on the oxygen affinity of human erythrocytes and hemoglobin. EUROPEAN JOURNAL OF BIOCHEMISTRY, 91(1), 285-289.
The effect of 2-methoxy-5-nitrotropone on the oxygen affinity of human erythrocytes and hemoglobin
CONDO', SAVERIO GIOVANNI;
1978-11-02
Abstract
Human hemoglobin reacted with 2-methoxy-5-nitrotropone at pH 7.4 undergoes modification of the four N-terminal amino groups. The modified protein shows increased oxygen affinity with complete abolition of the effect of K-glycerate 2, 3-bisphosphate. The Bohr effect is abolished in the acid range and drastically reduced at alkaline pH values. Changes in the kinetics of ligand reactions parallel the oxygen equilibrium results. Cooperative effects are still present. Human erythrocytes treated with 2-methoxy-5-nitrotropone show increased oxygen affinity and some decrease in methemoglobin reductase efficiency but no change in resistance to hemolysis.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
