Laurate and arachidonate omega and (omega-1)-hydroxylase activities, cytochrome P450 2E1 (CYP2E1), and CYP4A content were measured in 18 human kidney microsomal samples. The rates of laurate and arachidonate were found to be very different from those measured in human liver samples, with a laurate omega/omega-1 ratio of approximately 22 in human kidney vs 0.75 in human liver. Immunoblot analysis of the 18 human kidney microsomal samples identified 1 CYP4A electrophoretic band, but CYP2E1 was not detectable in human kidney, contrary to liver. Laurate and arachidonate omega-hydroxylase activities were significantly correlated with CYP4A content (r = 0.86 and 0.75, respectively). Polyclonal antirat CYP2E1 antibody did not affect omega-hydroxylase activity, whereas the polyclonal antirat CYP4A1 antibody inhibited it by 60%. These results suggest that, in contrast to other species, human kidney microsomes do not contain significant amounts of CYP2E1, but possess CYP4A and fatty acid omega-hydroxylase activity.