Purification of Cytochrome P450 BM-3 as a Monooxygenase
Authors: Jun, Huang; Lehe, Mei; Qing, Sheng; Dongqiang, Lin; Shanjing, Yao
Source: Protein and Peptide Letters, Volume 12, Number 4, May 2005 , pp. 327-331(5)
Publisher: Bentham Science Publishers
Abstract:After investigating two anion-exchange resins, the purification factor and activity yields of P450 BM-3 were higher with Resource Q than with DEAE-Sepharose FF. Screening of HIC media showed that Source 15ISO was the most suitable for purification of P450 BM-3. An effective isolation and purification procedure of P450 BM-3 was developed and included three steps: 35%-70% saturation (NH4)2SO4 precipitation, Source 15ISO hydrophobic interaction chromatograph and Sephacryl S-200 gel filtration chromatography. Using this protocol, the purification factor and P450 BM-3 activity recovery was 13.5 and 13.7%, respectively.
Document Type: Review Article
Affiliations: Department of Chemical and Biochemical Engineering, Zhejiang University, Hangzhou 310027 PR China.
Publication date: May 1, 2005
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.