di Ilio C, Sacchetta P, del Boccio G, la Rovere G, Federici G
Cancer Lett. 1985 Oct;29(1):37-42. doi: 10.1016/0304-3835(85)90120-x.
Glutathione peroxidase (GSH-Px), glutathione S-transferase (GSH-Tr) and glutathione reductase (GSSG-Rx) activities have been determined in normal and neoplastic human breast tissues. Large interindividual variations in the activities of all enzymes tested were found in both tumor and non-tumor specimens. In general a significant increase in the activities of the 3 enzymes was found in tumors, whereas in fibroadenoma they were as high as in healthy tissues. When a comparison was made between normal and neoplastic tissues of the same individual, GSH-Tr and GSSG-Rx activities were found to be higher in 15 and 11 cases, respectively, out of 17. GSG-Px activity was higher in all cases. From measurement of GSG-Px activity with both H202 and cumene hydroperoxide, it was deduced that human breast contains only the selenium-dependent form.
已测定正常和肿瘤性人类乳腺组织中的谷胱甘肽过氧化物酶（GSH-Px）、谷胱甘肽S-转移酶（GSH-Tr）和谷胱甘肽还原酶（GSSG-Rx）活性。在肿瘤和非肿瘤标本中均发现所检测的所有酶活性存在较大的个体间差异。总体而言，肿瘤中这3种酶的活性显著增加，而在纤维腺瘤中它们与健康组织中的活性一样高。当对同一个体的正常组织和肿瘤组织进行比较时，在17例中有15例GSH-Tr活性较高，11例GSSG-Rx活性较高。所有病例中GSG-Px活性均较高。通过用H202和氢过氧化异丙苯测定GSG-Px活性，推断出人类乳腺仅含有硒依赖型。
