The major nucleoside triphosphatase in pea (Pisum sativum L.) nuclei and in rat liver nuclei share common epitopes also present in nuclear lamins.
The major nucleoside triphosphatase in pea (Pisum sativum L.) nuclei and in rat liver nuclei share common epitopes also present in nuclear lamins.
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豌豆 (Pisum sativum L.) 细胞核和大鼠肝细胞核中的主要核苷三磷酸酶具有共同的表位，这些表位也存在于核纤层中。
DOI：
10.1104/pp.101.3.1005
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发表时间：
1993
期刊：
影响因子：
7.4
通讯作者：
Roux,SJ
中科院分区：
文献类型：
--
作者：
Tong,CG;Dauwalder,M;Clawson,GA;Hatem,CL;Roux,SJ
研究了哺乳动物和豌豆（PisumsativumL.）细胞核与酶相关，这些酶在生物化学和免疫化学上都非常相似。大鼠肝细胞核的主要NTR似乎是一种46 kD的酶，代表核纤层蛋白A和C的N-末端部分，这两种核纤层蛋白显然是通过选择性剪接从同一基因产生的。单克隆抗体（MAb）G2，提出了人类核纤层蛋白C，免疫沉淀的主要（47 kD）的NT α在豌豆核，并承认它在Western印迹分析。提出的47 kD豌豆NTR（pc 480）的多克隆抗体制剂与相同的核纤层蛋白带，在哺乳动物细胞核中的单克隆抗体G2识别反应。pc 480抗体还结合豌豆核基质制备物中的相同核纤层蛋白样条带，所述条带被G2和已知结合哺乳动物核纤层蛋白的三种其它MAb识别。在免疫荧光测定中，pc 480和抗核纤层蛋白抗体染色植物细胞中的细胞质和细胞核抗原，沿着细胞核的周边沿着有轻微增强的染色。这些结果表明豌豆和大鼠肝脏NTPases在结构上相似，并且在豌豆细胞核中与在大鼠肝细胞核中一样，主要的NTPases可能通过蛋白水解源自核纤层蛋白前体。
The major nucleoside triphosphatase (NTPase) activities in mammalian and pea (Pisum sativum L.) nuclei are associated with enzymes that are very similar both biochemically and immunochemically. The major NTPase from rat liver nuclei appears to be a 46-kD enzyme that represents the N-terminal portion of lamins A and C, two lamina proteins that apparently arise from the same gene by alternate splicing. Monoclonal antibody (MAb) G2, raised to human lamin C, both immunoprecipitates the major (47 kD) NTPase in pea nuclei and recognizes it in western blot analyses. A polyclonal antibody preparation raised to the 47-kD pea NTPase (pc480) reacts with the same lamin bands that are recognized by MAb G2 in mammalian nuclei. The pc480 antibodies also bind to the same lamin-like bands in pea nuclear envelope-matrix preparations that are recognized by G2 and three other MAbs known to bind to mammalian lamins. In immunofluorescence assays, pc480 and anti-lamin antibodies stain both cytoplasmic and nuclear antigens in plant cells, with slightly enhanced staining along the periphery of the nuclei. These results indicate that the pea and rat liver NTPases are structurally similar and that, in pea nuclei as in rat liver nuclei, the major NTPase is probably derived from a lamin precursor by proteolysis.