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. Author manuscript; available in PMC: 2007 Sep 25.

Published in final edited form as: Biochemistry. 2006 Dec 26;45(51):15807–15816. doi: 10.1021/bi061803n

CYP2E1, CYP2B4 and reductase were reconstituted in binary (reductase and a single P450) and ternary (reductase and mixed P450s) systems. Significant differences in activities between the sum of the two binary systems compared to the mixed reconstituted system are indicated (*, p < 0.05). Calculated ionic strength values for each buffer system are indicated as the top x-axis. PROD activities were measured at varying concentrations of (a) HEPES/acetate and (b) HEPES buffer. Reaction conditions are the same as described in Fig 2. Bars represent the mean ± SEM for three determinations.

CYP2E1, CYP2B4 and reductase were reconstituted in binary (reductase and a single P450) and ternary (reductase and mixed P450s) systems. Significant differences in activities between the sum of the two binary systems compared to the mixed reconstituted system are indicated (*, p < 0.05). Calculated ionic strength values for each buffer system are indicated as the top x-axis. PROD activities were measured at varying concentrations of (a) HEPES/acetate and (b) HEPES buffer. Reaction conditions are the same as described in Fig 2. Bars represent the mean ± SEM for three determinations.