Localization of manganese superoxide dismutase in peroxisomes isolated from Pisum sativum L.
Localization of manganese superoxide dismutase in peroxisomes isolated from Pisum sativum L.
复制标题
从豌豆分离的过氧化物酶体中锰超氧化物歧化酶的定位。
DOI：
10.1016/0168-9452(87)90213-5
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发表时间：
1987
期刊：
影响因子：
5.2
通讯作者：
L. A. Río
中科院分区：
文献类型：
--
作者：
L. Sandalio;J. Palma;L. A. Río
豌豆叶片过氧化体中金属酶超氧化物歧化酶的存在。对其进行了研究。用差速离心法和Percoll密度梯度离心法分离植物细胞器。纯化的完整过氧化物体含有一种超氧化物歧化酶同工酶，经聚丙烯酰胺凝胶分析和对KCN-和H_2O_2的敏感性鉴定为含锰超氧化物歧化酶(Mn-SOD)。通过测定完整的过氧化物体中超氧化物歧化酶活性的潜伏期，证明了Mn-SOD位于这些氧化细胞器的内部。就比活性而言，线粒体中的过氧化物型锰超氧化物歧化酶至少占整个超氧化物歧化酶活性的50%。过氧化酶体中锰超氧化物歧化酶的存在强烈地表明，在这些氧化细胞器中产生了酶的底物超氧阴离子自由基(O2.−)，以及细胞代谢中与氧有关的新的激活功能。
The presence of the metalloenzyme superoxide dismutase (SOD) in peroxisomes from leaves ofPisum sativumL. was studied. Plant organelles were isolated by differential and Percoll density-gradient centrifugation. Purified intact peroxisomes contained a superoxide dismutase isozyme which was identified, on the basis of polyacrylamide-gel analysis and KCN- and H2O2-sensitivity, as a Mn-containing SOD (Mn-SOD). By determination of latency of superoxide dismutase activity in intact peroxisomes, Mn-SOD was demonstrated to be located in the interior of these oxidative organelles. In terms of specific activity, the peroxisomal Mn superoxide dismutase represents at least 50% of the whole SOD activity occurring in mitochondria. The presence of a Mn-SOD in peroxisomes strongly suggests the generation in these oxidative organelles of superoxide free radicals (O2.−), the substrate of the enzyme, as well as new activated oxygen-related functions for peroxisomes in cellular metabolism.