Adrenocorticotropic hormone (ACTH) is an old medicine derived from porcine pituitary gland that has been marketed for more than 60 years. In this study, we present a recombinant approach to produce ACTH in Escherichia coli (E. coli). The SUMO-tagged fusion protein was cloned and expressed after induction with isopropyl-β-d-thiogalactopyranoside (IPTG) at 25 °C for 8 h. The fusion protein was extracted and purified by anion exchange chromatography, and the SUMO tag was subsequently removed by digestion with ubiquitin-like protease 1 (ULP1). Approximately 95.3 mg of recombinant ACTH with 94.2% purity was obtained after cation exchange purification performed on a 5 mL column, from 286 mL fermentation broth based on the amount of pellets homogenized. The molecular mass of the recombinant ACTH was confirmed by mass spectrometry to equal 4567.32 Da.

促肾上腺皮质激素（ACTH）是衍生自猪垂体的一种古老药物，已上市60多年。在这项研究中，我们提出了在大肠杆菌（E. coli）中生产ACTH的重组方法。异丙基-β - d-硫代半乳糖吡喃糖苷诱导后克隆并表达SUMO标签的融合蛋白（IPTG）在25°C下放置8小时。提取融合蛋白，并通过阴离子交换色谱纯化，然后通过用泛素样蛋白酶1（ULP1）消化除去SUMO标签。在5 mL色谱柱上进行阳离子交换纯化后，基于均质沉淀物的量，从286 mL发酵液中获得了约95.3 mg纯度为94.2％的重组ACTH。通过质谱法证实重组ACTH的分子量等于4567.32Da。