Oxidation reactions of human, opossum (Didelphis virginiana) and spot (Leiostomus xanthurus) hemoglobins: a search for a correlation with some structural-functional properties.
1. Relative to human HbA, opossum (Didelphis virginiana) hemoglobin was found to be more susceptible to autoxidation. While the initial rate of autoxidation of spot (Leiostomus xanthurus) hemoglobin is close to that of HbA, complete oxidation occurs in 50 hr. 2. Direct addition of hydrogen peroxide (H2O2) induced oxidation of hemoglobins in a definite order: spot Hb > HbA > opossum Hb. Excess H2O2 led to heme degradation and precipitation that occurred much faster for spot Hb than the case with other proteins. 3. Exposure of hemoglobins to a continuous flux of H2O2, generated by the glucose/glucose oxidase system, induced the formation of heterogeneous protein-associated oxidation products. 4. Differential reactivity among these hemoglobins under the same or different oxidative conditions, with respect to methemoglobin formation and stability of the ferric form, may reflect the differences in the local heme environment of these proteins.
Alayash
A I
AI
Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892.
Ryan
B A
BA
Fratantoni
J C
JC
D000222:Adaptation, Physiological; D000818:Animals; D005399:Fishes / Q000097:blood*; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D009893:Opossums / Q000097:blood*; D010084:Oxidation-Reduction; D013329:Structure-Activity Relationship
D006454:Hemoglobins