AbstractMicrosomal cytochrome P450 from tulip bulbs was solubilized and purified to a specific content of 12.66 nmol mg protein−1. The cytochrome P450 was present as a mixture of two cytochrome P450 polypeptides in approximately equal proportions. Their molecular masses were 52.5 kD and 54.5 kD. Similarities between these proteins included cross‐reactivity with the same antibody. Activity of the purified sample was investigated in a reconstituted enzyme system using the herbicide 2,4‐D (2,4‐dichlorophenoxyacetic acid) as a substrate. A polar product of 2,4‐D was produced which co‐migrated on several chromatography systems with 2,4‐d
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