Gabbianelli R, Santroni A M, Fedeli D, Kantar A, Falcioni G
Dipartimento di Biologia Molecolare, Cellulare e Animale, Università degli Studi di Camerino, Italia.
Biochem Biophys Res Commun. 1998 Jan 26;242(3):560-4. doi: 10.1006/bbrc.1997.7928.
The antioxidant activity of hemoglobin was examined by studying both its peroxidase activity and its interaction with the superoxide anion. The peroxidase activity of both the subunits (alpha and beta) was reduced with respect to the alpha 2 beta 2 tetramer and heme-oxidation was found to be associated with a decrease in this activity. Lucigenin-amplified chemiluminescence experiments have shown that at low pH, the presence of hemoglobin reduces the level of superoxide anion generated by the xanthine/xanthine oxidase system (met-Hb is more efficient in reducing the level of O2- than oxy-hemoglobin). These results confirm that hemoglobin may be of importance in providing protection against oxidative damage to erythrocytes.
通过研究血红蛋白的过氧化物酶活性及其与超氧阴离子的相互作用，对其抗氧化活性进行了检测。相对于α2β2四聚体，两个亚基（α和β）的过氧化物酶活性均降低，并且发现血红素氧化与该活性的降低有关。光泽精增强化学发光实验表明，在低pH值下，血红蛋白的存在会降低黄嘌呤/黄嘌呤氧化酶系统产生的超氧阴离子水平（高铁血红蛋白在降低O2-水平方面比氧合血红蛋白更有效）。这些结果证实，血红蛋白在提供针对红细胞氧化损伤的保护方面可能具有重要意义。
