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- W2134368304 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 (NH(4))(2)SO(4) 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." @default.
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- W2134368304 date "2005-05-01" @default.
- W2134368304 modified "2023-09-26" @default.
- W2134368304 title "Purification of Cytochrome P450 BM-3 as a Monooxygenase" @default.
- W2134368304 doi "https://doi.org/10.2174/0929866053765653" @default.
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