Olsen R L, Little C
Eur J Biochem. 1979 Nov;101(2):333-9. doi: 10.1111/j.1432-1033.1979.tb19725.x.
The peroxidase activity in the uterine extract of rats previously given a low dose of oestradiol has been examined. From sexually mature rats, two peroxidases of apparent molecular weights of 92 000 (peroxidase I) and 40 000 (peroxidase II) and of different mobilities in polyacrylamide disc gel electrophoresis were found. The two peroxidases were separated and characterized in terms of their substrate specificities, kinetics, pH optima for activity, inhibitors and stabilities. Both enzymes appeared to be classic haemoprotein peroxidases of very similar properties. Peroxidase II was further purified.
对先前给予低剂量雌二醇的大鼠子宫提取物中的过氧化物酶活性进行了检测。从性成熟大鼠中,发现了两种过氧化物酶,其表观分子量分别为92000(过氧化物酶I)和40000(过氧化物酶II),并且在聚丙烯酰胺圆盘凝胶电泳中具有不同的迁移率。对这两种过氧化物酶进行了分离,并根据它们的底物特异性、动力学、活性的最适pH值、抑制剂和稳定性进行了表征。这两种酶似乎都是性质非常相似的典型血红蛋白过氧化物酶。过氧化物酶II得到了进一步纯化。