Plant Physiol. Illumina
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Plant Physiology 89:1141-1149 (1989)
© 1989 American Society of Plant Biologists

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Metabolism and Enzymology

Cytochrome P-450 from the Mesocarp of Avocado (Persea americana)

Daniel P. O'Keefe and Kenneth J. Leto1

Department of Central Research and Development, E. I. du Pont de Nemours and Company, Inc., Experimental Station, P.O. Box 80402, Wilmington, Delaware 19880-0402, Department of Agricultural Products, E. I. du Pont de Nemours and Company, Inc., Experimental Station, P.O. Box 80402, Wilmington, Delaware 19880-0402

The microsomal fraction from the mesocarp of avocado (Persea americana) is one of few identified rich sources of plant cytochrome P-450. Cytochrome P-450 from this tissue has been solubilized and purified. Enzymatic assays (p-chloro-N-methylaniline demethylase) and spectroscopic observations of substrate binding suggest a low spin form of the cytochrome, resembling that in the microsomal membrane, can be recovered. However, this preparation of native protein is a mixture of nearly equal proportions of two cytochrome P-450 polypeptides that have been resolved only under denaturing conditions. Overall similarities between these polypeptides include indistinguishable amino acid compositions, similar trypsin digest patterns, and cross reactivity with the same antibody. The amino terminal sequences of both polypeptides are identical, with the exception that one of them lacks a methionine residue at the amino terminus. This sequence exhibits some similarities with the membrane targeting signal found at the amino terminus of most mammalian cytochromes P-450.

1 Current address: Agricultural Products Department, E. I. du Pont Company, Stine Research Laboratories, Newark, DE 19714.




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