Purification of Cytochrome P450 BM-3 as a Monooxygenase

Title: Purification of Cytochrome P450 BM-3 as a Monooxygenase

Volume: 12 Issue: 4

Author(s): Huang Jun, Mei Lehe, Sheng Qing, Lin Dongqiang and Yao Shanjing

Affiliation:

Keywords: p bm, purification, ion-exchange chromatography, hydrophobic-interaction chromatography, gel filtration chromatography

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.

Cite this article as:

Jun Huang, Lehe Mei, Qing Sheng, Dongqiang Lin and Shanjing Yao, Purification of Cytochrome P450 BM-3 as a Monooxygenase, Protein & Peptide Letters 2005; 12 (4) . https://dx.doi.org/10.2174/0929866053765653