两种卟啉合成酶在豌豆和海芋属植物中的亚细胞定位
Subcellular localization of two porphyrin-synthesis enzymes in Pisum sativum (pea) and Arum (cuckoo-pint) species.
作者信息
Smith A G
机构信息
Department of Botany, University of Cambridge, U.K.
出版信息
Biochem J. 1988 Jan 15;249(2):423-8. doi: 10.1042/bj2490423.
Abstract
The subcellular location of the two porphyrin-synthesis enzymes 5-aminolaevulinate dehydratase (ALAD) and porphobilinogen deaminase (PBGD) was investigated in Pisum sativum (pea) leaves and spadices of Arum (cuckoo-pint). Throughout the tissue-fractionation procedures the distribution of the two enzymes paralleled that of the plastid marker enzyme (ADP-glucose pyrophosphorylase), even in Arum, a tissue where the synthesis of non-plastid haem is predominant. The distribution of cytosolic marker enzyme (lactate dehydrogenase) was significantly different from that of ALAD and PBGD and, although purified mitochondria from both species had some residual activity, this was always less than contaminating plastid marker enzyme. The results suggest that ALAD and PBGD are exclusively plastid enzymes. The significance of this for the role of plastids in cellular porphyrin synthesis is discussed.
摘要
在豌豆叶片和海芋（白星海芋）肉穗花序中研究了两种卟啉合成酶，即5-氨基乙酰丙酸脱水酶（ALAD）和胆色素原脱氨酶（PBGD）的亚细胞定位。在整个组织分级分离过程中，这两种酶的分布与质体标记酶（ADP-葡萄糖焦磷酸化酶）的分布平行，即使在海芋这种非质体血红素合成占主导的组织中也是如此。胞质标记酶（乳酸脱氢酶）的分布与ALAD和PBGD的分布显著不同，并且，尽管来自这两个物种的纯化线粒体有一些残余活性，但这总是低于污染的质体标记酶的活性。结果表明，ALAD和PBGD是专门的质体酶。文中讨论了这对于质体在细胞卟啉合成中的作用的意义。
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