Purification and herbicide metabolism studies on tulip (Tulipa gesneriana) cytochrome P450
1993
Topal, A. | Adams, N. | Dauterman, W.C. | Hodgson, E. | Kelly, S.L.
Microsomal 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-dichlorophenol.
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