Purification and characterization of an ascorbate peroxidase from potato tuber mitochondria
Purification and characterization of an ascorbate peroxidase from potato tuber mitochondria
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DOI：
10.1016/s0981-9428(00)01188-8
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发表时间：
2000-10-01
影响因子：
6.5
通讯作者：
Dipierro, S
中科院分区：
文献类型：
--
作者：
De Leonardis, S;Dipierro, N;Dipierro, S
从马铃薯块茎(Solanum tuberosum L.)中纯化出抗坏血酸过氧化物酶(APX)。线粒体。土豆酶似乎定位在线粒体内。对线粒体APX进行了纯化，比较了其与胞浆酶的物理化学和动力学性质。经SDS-PAGE测定，mAPX的相对分子质量为31 kDa，与胞浆酶相似，但在非变性PAGE中的相对迁移率不同于胞浆APX。AsA和H_2O_2对mAPX的K-m值分别为76.1+/-23.1和80.3+/-24.9微米，均高于胞浆酶。线粒体APX对巯基试剂汞和对羟基苯甲酸汞(p-HMB)的抑制作用敏感。提出了线粒体抗坏血酸-抗坏血酸过氧化物酶系统在清除马铃薯块茎线粒体内有毒氧物种中的作用。(C)2000年版《爱思唯尔科学与医学》。
Ascorbate peroxidase (APX) has been purified from potato tuber (Solanum tuberosum L.) mitochondria. The potato enzyme appeared to be localized inside mitochondria. The mitochondrial APX was purified to homogeneity and its physico-chemical and kinetic propel-ties were compared with those of the cytosolic enzyme. The molecular mass of mAPX was 31 kDa, as estimated by SDS-PAGE, and was similar to that of the cytosolic enzyme, but its relative mobility in non-denaturing PAGE was different from the cytosolic APX. The K-m values of mAPX for AsA and H2O2 were 76.1 +/- 23.1 and 80.3 +/- 24.9 muM, respectively, and were higher than those of the cytosolic enzyme. Mitochondrial APX was sensitive to inhibition by sulfhydryl reagents, such as mersalyl and p-hydroxymercuribenzoate (p-HMB). A role for the mitochondrial ascorbate-ascorbate peroxidase system in the scavenging of toxic oxygen species inside potato tuber mitochondria is proposed. (C) 2000 Editions scientifiques et medicales Elsevier SAS.