Ribeiro O, Kirkby C A, Hirom P C, Millburn P
Carcinogenesis. 1986 Mar;7(3):481-4. doi: 10.1093/carcin/7.3.481.
3-Hydroxybenzo[a]pyrene (3-OH-BaP) is oxidized by the horseradish peroxidase/H2O2 system to benzo[a]pyrene-3,6-quinone. In the presence of N-acetylcysteine one other product is also formed. This was identified by its chemical, and u.v., mass and n.m.r. spectral properties as 6-(H-acetyl-cystein-S-yl)-3-hydroxybenzo[a]pyrene (6-NAc-cys-3-OH-BaP). Replacement of the N-acetylcysteine by glutathione leads to the formation of a 3-OH-BaP-glutathione adduct. Enzymic hydrolysis of benzo[a]pyrene-3-glucuronide in the presence of N-acetylcysteine yields, in addition to 3-OH-BaP, a product which co-chromatographs with 6-NAc-cys-3-OH-BaP and has identical chemical and spectral characteristics.
3-羟基苯并[a]芘（3-OH-BaP）被辣根过氧化物酶/H₂O₂体系氧化为苯并[a]芘-3,6-醌。在N-乙酰半胱氨酸存在的情况下，还会形成另一种产物。通过其化学、紫外、质谱和核磁共振光谱性质鉴定该产物为6-(H-乙酰-半胱氨酸-S-基)-3-羟基苯并[a]芘（6-NAc-cys-3-OH-BaP）。用谷胱甘肽替代N-乙酰半胱氨酸会导致形成3-OH-BaP-谷胱甘肽加合物。在N-乙酰半胱氨酸存在下，苯并[a]芘-3-葡萄糖醛酸苷的酶促水解除了产生3-OH-BaP外，还产生一种与6-NAc-cys-3-OH-BaP共色谱且具有相同化学和光谱特征的产物。
