Sonmez Gamze, Karatas Bahattin Enes, Bodur Ebru
Department of Medical Biochemistry, Hacettepe University Faculty of Medicine, Ankara, Turkey.
Protein J. 2025 Feb 7. doi: 10.1007/s10930-025-10248-x.
Butyrylcholinesterase (BChE; EC 3.1.1.8) is an enzyme found in blood plasma and various tissues, playing a key role in metabolizing esters and detoxifying various substances. In this study, we developed a modified purification protocol for BChE from human serum, achieving a higher purification yield (38.3%) and specific activity (60,500 U/mg) compared to previous reports. The method employed a single round of acid dialysis, Sephadex G50 gel filtration chromatography, and procainamide Sepharose 4 fast flow affinity chromatography. Our new approach excludes the commonly used DEAE Trisacryl M chromatography. The goal was to compare this method with our previously employed purification protocols. This study demonstrates that optimizing chromatography steps can enhance enzyme recovery and activity, though further refinement may be needed for higher purification folds. This improved methodology offers a valuable approach for efficient BChE purification with potential for broader applications.
丁酰胆碱酯酶（BChE；EC 3.1.1.8）是一种存在于血浆和各种组织中的酶，在酯类代谢和多种物质解毒过程中发挥关键作用。在本研究中，我们开发了一种从人血清中纯化BChE的改良方案，与之前的报道相比，实现了更高的纯化产率（38.3%）和比活性（60,500 U/mg）。该方法采用了一轮酸透析、Sephadex G50凝胶过滤色谱和普鲁卡因酰胺琼脂糖4快速流动亲和色谱。我们的新方法排除了常用的DEAE Trisacryl M色谱。目的是将该方法与我们之前采用的纯化方案进行比较。本研究表明，优化色谱步骤可以提高酶的回收率和活性，不过为了获得更高的纯化倍数可能还需要进一步改进。这种改进的方法为高效纯化BChE提供了一种有价值的途径，具有更广泛的应用潜力。
