Lim Y S, Cha M K, Kim H K, Uhm T B, Park J W, Kim K, Kim I H
Department of Biochemistry, Pai-Chai University, Taejon, Republic of Korea.
Biochem Biophys Res Commun. 1993 Apr 15;192(1):273-80. doi: 10.1006/bbrc.1993.1410.
Thiol-specific antioxidant protein (Protector Protein; PRP) from Saccharomyces cerevisiae was found to remove hydrogen peroxide and hydroxyl radical in the presence of dithiothreitol (DTT). Without DTT as a reducing equivalent, the antioxidant protein did not show the activities for destroying hydrogen peroxide and hydroxyl radical. N-ethylmaleimide (NEM) was observed to prevent the PRP from both removing hydrogen peroxide and protecting the cleavage of DNA. These observations suggest that the sulfhydryl of cysteine in PRP could function as a strong nucleophile to attack and destroy H2O2 and .OH.
发现来自酿酒酵母的硫醇特异性抗氧化蛋白(保护蛋白;PRP)在二硫苏糖醇(DTT)存在的情况下能够清除过氧化氢和羟基自由基。在没有DTT作为还原当量的情况下,该抗氧化蛋白未表现出破坏过氧化氢和羟基自由基的活性。观察到N-乙基马来酰亚胺(NEM)可阻止PRP清除过氧化氢和保护DNA的裂解。这些观察结果表明,PRP中半胱氨酸的巯基可作为强亲核试剂攻击并破坏H2O2和·OH。