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. Author manuscript; available in PMC: 2016 Jul 1.
Published in final edited form as: Prostaglandins Other Lipid Mediat. 2015 May 15;120:40–49. doi: 10.1016/j.prostaglandins.2015.05.004

Table 1. Rates of EET ω-hydroxylation by purified recombinant rat CYP4A proteins.

Enzymatic activities were reconstituted in the presence of dilauroylphosphatidylcholine (50 mg/ml), by mixing each P450 enzyme with cytochrome b5 and cytochrome P450 oxido-reductase in 1:1:10 molar ratio. Reactions were carried out at 35° in Tris-Cl buffer pH 7.4 containing 10 mM MgCl2, 0.1 M KCl, and 1 mM NADPH. Organic soluble products were resolved by reversed phase HPLC and quantified by on-line β detection (60). Shown are average Kcat values ±SE (in min-1) calculated from time courses of product formation vs incubation time.

Protein 8,9-EET 11, 12-EET 14, 15-EET
CYP4A1 15.0 ±0.9 10.0 ±0.5 4.0 ±0.1
CYP4A2 4.0 ±0.2 7.0 ±0.4 3.0 ±0.3
CYP4A8 0.8 ±0.2 1.3 ±0.1 0.8 ±0.1