Leucine aminopeptidase from etiolated barley seedlings: characterization and partial purification of isoforms
Leucine aminopeptidase from etiolated barley seedlings: characterization and partial purification of isoforms
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DOI：
10.1016/j.plantsci.2004.08.007
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发表时间：
2005-03-01
期刊：
影响因子：
5.2
通讯作者：
Shioi, Y
中科院分区：
文献类型：
--
作者：
Ogiwara, N;Amano, T;Shioi, Y
亮氨酸氨基肽酶(LAP)是一种催化蛋白质周转循环的末端酶。来自植物的LAP的正常性质显示出六面体结构，热稳定性超过60摄氏度，最适pH约为9.5。从黄化大麦幼苗中分离到三种类型的LAP，分别命名为LAP 1、LAP 2和LAP 3，亚基组成均为57 kDa的单体结构。LAP 1、LAP 2和LAP 3的热稳定性由最大活性的50%的酶表示，分别为51℃、54℃和56℃。LAP 1和LAP 2的最适pH为7.0，LAP 3的最适pH为8.0。黄化苗和绿苗的叶组织、胚芽鞘和根中的LAP活性基本相同。所有圈数对对氯汞苯甲酸敏感。与其他植物物种的LAPS相比，大麦幼苗的LAPS提供了新的特性。(C)2004爱思唯尔爱尔兰有限公司。保留所有权利。
Leucine aminopeptidase (LAP) is a terminal enzyme catalyzing a cycle of protein turnover. The normal properties of LAP from plants show a hexameric structure, thermostability over 60 degreesC and optimum pH of approximately 9.5. We isolated three types of LAP from etiolated barley seedlings, which were designated as LAP 1, LAP 2 and LAP 3. All of the subunit compositions were 57 kDa of monomeric structure. The thermostability, of LAP 1, LAP 2 and LAP 3 was indicated by the enzymes having 50% of maximum activities, 51, 54 and 56 degreesC, respectively. The optimum pH was 7.0 for LAP 1 and LAP 2, and 8.0 for LAP 3. LAP activity was found almost equally in leaf tissue, coleoptile and roots from etiolated and green seedlings. All LAPs were sensitive to p-chloromercuribenzoic acid. LAPs from barley seedlings provide novel properties compared to LAPs from other plant species. (C) 2004 Elsevier Ireland Ltd. All rights reserved.