Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy.
Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy.
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DOI：
10.1083/jcb.79.1.10
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发表时间：
1978-10
影响因子：
7.8
通讯作者：
Chrispeels, M J
中科院分区：
文献类型：
--
作者：
Baumgartner, B;Tokuyasu, K T;Chrispeels, M J
豌豆球蛋白肽水解酶是一种蛋白酶，可水解绿豆 (Vigna radiata) 幼苗子叶中的储备蛋白，已使用针对该酶的单特异性抗体和罗丹明偶联的山羊抗兔免疫球蛋白 G 通过免疫荧光显微镜将其定位在细胞内。该酶在幼苗生长 3 天后首次可见，并且与距维管束最远的储存薄壁细胞的细胞质内的小焦点相关。在生长的第四天，蛋白酶也存在于这些细胞内的众多大蛋白体中。已知豌豆球蛋白肽水解酶从生长的第三天开始合成。因此，我们的观察结果与酶在细胞质中合成并随后转运至蛋白体的解释一致。
Vicilin peptidohydrolase, the protease that hydrolyzes the reserve proteins in the cotyledons of mung bean (Vigna radiata) seedlings, has been localized intracellularly by immunofluorescence microscopy using monospecific antibodies against the enzyme and rhodamine-coupled goat- anti-rabbit immunoglobulin G's. The enzyme can first be visualized after 3 days of seedling growth and is associated with small foci within the cytoplasm of the storage parenchyma cells farthest from the vascular bundles. On the 4th day of growth, the protease is also present in the numerous large protein bodies within these cells. Vicilin peptidohydrolase is known to be synthesized de novo starting on the 3rd day of growth. Our observations are therefore consistent with the interpretation that the enzyme is synthesized in the cytoplasm and subsequently transported to the protein bodies.