两种植物蛋白的克隆与表达：天然形式与重组形式具有相似的抗菌活性。
Cloning and expression of two plant proteins: similar antimicrobial activity of native and recombinant form.
作者信息
Capparelli R, Palumbo D, Iannaccone M, Ventimiglia I, Di Salle E, Capuano F, Salvatore P, Amoroso M G
机构信息
School of Biotechnological Sciences, University of Naples Federico II, Via Università 133, Portici, Naples 80055, Italy.
出版信息
Biotechnol Lett. 2006 Jul;28(13):943-9. doi: 10.1007/s10529-006-9031-9. Epub 2006 Jun 23.
Antimicrobial peptides and proteins are being studied with increasing interest because of their broad range antimicrobial activity. Among plant antimicrobial proteins, the wheat seed polypeptides, puroindoline a and puroindoline b, are particularly interesting because of their established antibacterial activity. In this paper we describe different strategies used to clone His tagged and GST tagged puroindolines obtaining 1.5 mg recombinant protein from 1 l culture. The antimicrobial activity of recombinant and native puroindolines was comparable.
由于抗菌肽和蛋白质具有广泛的抗菌活性，它们正受到越来越多的关注。在植物抗菌蛋白中，小麦种子多肽麦醇溶蛋白a和麦醇溶蛋白b因其已确定的抗菌活性而特别引人关注。在本文中，我们描述了用于克隆带有组氨酸标签和谷胱甘肽-S-转移酶标签的麦醇溶蛋白的不同策略，从1升培养物中获得了1.5毫克重组蛋白。重组麦醇溶蛋白和天然麦醇溶蛋白的抗菌活性相当。
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