Plesnicar M, Bonner W D, Storey B T
Plant Physiol. 1967 Mar;42(3):366-70. doi: 10.1104/pp.42.3.366.
The presence of peroxidase in mitochondria from etiolated mung bean hypocotyls and skunk cabbage spadices, suggested by carbon monoxide difference spectra and the spectral response to methyl hydroperoxide, was shown to result from contamination of the isolated mitochondria by a denser particle fraction with high peroxidase activity. The mitochondria themselves have no peroxidatic activity. Analysis of the homogenate of mung bean hypocotyls revealed that over 90% of the peroxidase was soluble, as expected. Sonication of the isolated mitochondria, however, did not remove all the peroxidase from the particulate fraction, indicating that some of this enzyme is tightly bound to a membrane. These results suggest that the peroxidase in plant cells is localized in lysosomes or microbodies, most of which are ruptured on tissue homogenization to give soluble peroxidase, but some of which survive and appear as membrane bound peroxidase.
通过一氧化碳差光谱以及对氢过氧化甲基的光谱响应表明，黄化绿豆下胚轴和臭菘佛焰苞的线粒体中存在过氧化物酶，但结果显示，分离得到的线粒体中存在过氧化物酶是由于被具有高过氧化物酶活性的更致密颗粒组分污染所致。线粒体本身没有过氧化物酶活性。正如预期的那样，对绿豆下胚轴匀浆的分析表明，超过90%的过氧化物酶是可溶的。然而，对分离得到的线粒体进行超声处理并没有从颗粒组分中去除所有的过氧化物酶，这表明这种酶的一部分与膜紧密结合。这些结果表明，植物细胞中的过氧化物酶定位于溶酶体或微体中，其中大部分在组织匀浆时破裂，产生可溶性过氧化物酶，但也有一些存活下来并表现为膜结合过氧化物酶。
