人类、负鼠（弗吉尼亚负鼠）和斑点原鮨血红蛋白的氧化反应：探寻与某些结构功能特性的相关性。

Oxidation reactions of human, opossum (Didelphis virginiana) and spot (Leiostomus xanthurus) hemoglobins: a search for a correlation with some structural-functional properties.

Alayash A I, Ryan B A, Fratantoni J C

Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892.

Comp Biochem Physiol B. 1993 Oct;106(2):427-32. doi: 10.1016/0305-0491(93)90324-x.

Abstract

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.

摘要

相对于人类血红蛋白A（HbA），发现负鼠（弗吉尼亚负鼠）血红蛋白更容易发生自氧化。虽然斑点原鮨血红蛋白的初始自氧化速率与HbA接近，但在50小时内会完全氧化。2. 直接添加过氧化氢（H2O2）会以一定顺序诱导血红蛋白氧化：斑点原鮨血红蛋白> HbA>负鼠血红蛋白。过量的H2O2会导致血红素降解和沉淀，斑点原鮨血红蛋白发生这种情况的速度比其他蛋白质快得多。3. 将血红蛋白暴露于由葡萄糖/葡萄糖氧化酶系统产生的连续H2O2流中，会诱导形成异质的蛋白质相关氧化产物。4. 在相同或不同氧化条件下，这些血红蛋白在高铁血红蛋白形成和三价铁形式稳定性方面的反应性差异，可能反映了这些蛋白质局部血红素环境的差异。