NOVEL PROCESS FOR SOLUBILIZING INCLUSION BODIES

重组DNA技术的一个重大发展是 在原核生物中表达真核基因的能力，如 大肠埃希菌。由于许多真核生物的天然供应 具有潜在临床或工业重要性的蛋白质是有限的， 基因克隆和表达提供了潜在的丰富来源 真核蛋白质。 在原核生物中表达的重组蛋白被隔离在 细胞质为不可溶的聚集体，称为包涵体。 目前，从包涵体中回收重组蛋白 身体需要使用具有侵略性的蛋白质变性剂 会对蛋白质造成不可逆转的损害，并产生非常低的百分比 活性蛋白质。 在这项建议中，我们描述了一种新的增溶和 从包涵体中回收真核蛋白。这个过程 承诺取代或增强增溶和回收 当前正在使用的进程。主要的预期收益是 以其活性形式提高蛋白质的产量。

A significant development in recombinant dna technology is the capability to express eukaryotic genes in prokaryotes such as Escherichia coli. Since the natural supply of many eukaryotic proteins of potential clinical or industrial importance is limited, gene cloning and expression offer a potentially abundant source of eukaryotic proteins. Recombinant proteins expressed in prokaryotes are sequestered in the cytoplasm as insoluble aggregates known as inclusion bodies. Currently, the recovery of recombinant proteins from inclusion bodies requires the use aggressive protein denaturing agents that can irreversibly damage the protein and yields very low percentages of active protein. In this proposal, we describe a novel process for solubilizing and recovering eukaryotic proteins from inclusion bodies. The process promises to replace or enhance the solubilization and recovery process currently in use. The principal expected benefit is an improvement in the yield of protein in its active form.