From Crude Extracts to Purity: A Comparative Study of Butyrylcholinesterase Purification

Sonmez G., Karatas B. E., BODUR E.

PROTEIN JOURNAL, 2025 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Basım Tarihi: 2025
  • Doi Numarası: 10.1007/s10930-025-10248-x
  • Dergi Adı: PROTEIN JOURNAL
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Chemical Abstracts Core, MEDLINE, Veterinary Science Database
  • Hacettepe Üniversitesi Adresli: Evet

Özet

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.