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首页> 外文期刊>Online journal of biological sciences >Subcellular Localization Studies of Three Phenylalanine Ammonia-Lyases and Cinnamate 4-Hydroxylase from Scutellaria Baicalensis Using GFP Fusion Proteins
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Subcellular Localization Studies of Three Phenylalanine Ammonia-Lyases and Cinnamate 4-Hydroxylase from Scutellaria Baicalensis Using GFP Fusion Proteins

机译:利用GFP融合蛋白对黄S中的三种苯丙氨酸氨化酶和肉桂酸4-羟化酶进行亚细胞定位研究

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摘要

The localization of three phenylalanine ammonia-lyases (PALI, -2 and -3) and Cinnamate 4-Hydroxlase (C4H) of Scutellaria baicalensis was examined in onion epidermal cells. These genes encode key enzymes in the phenylpropanoid pathway for the synthesisof flavones. In our previous research, we isolated coding DNA for these genes from S. baicalensis, a medicinal herb rich in flavones with biological and pharmacological properties. We observed that SbPAL2, SbPAL3 and SbC4H proteins localize to the endoplasmic reticulum; however, SbPALl was a cytosolic protein. Unlike SbPAL2 and SbPAL3, SbPALl may be expected to have a different function in the flavone biosynthetic pathway.
机译:在洋葱表皮细胞中检查了黄ba的三种苯丙氨酸解氨酶(PALI,-2和-3)和肉桂酸4-羟化酶(C4H)的定位。这些基因编码苯丙烷类途径中合成黄酮的关键酶。在我们先前的研究中,我们从黄ical(S。baicalensis)中分离了这些基因的编码DNA,黄ical是一种富含黄酮的具有生物和药理特性的药用植物。我们观察到SbPAL2,SbPAL3和SbC4H蛋白定位于内质网。然而,SbPAL1是胞质蛋白。与SbPAL2和SbPAL3不同,可以预期SbPAL1在黄酮生物合成途径中具有不同的功能。

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