Cytochrome P-450 from the mesocarp of avocado (Persea americana)

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 subs...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1989-04, Vol.89 (4), p.1141-1149
Main Authors: O'Keefe, D.P. (E.I. du Pont de Nemours and Company, Inc., Wilmington, DE), Leto, K.J
Format: Article
Language:English
Subjects:
Amino acids
Anions
Biological and medical sciences
Cell biochemistry
Cell physiology
CHROMATOGRAPHIE
CHROMATOGRAPHIE LIQUIDE HAUTE PRESS
CROMATOGRAFIA
CROMATOGRAFIA LIQUIDA ALTA PRESION
Cytochromes
Detergents
ELECTROFORESIS
ELECTROPHORESE
Enzymes
FRUIT
FRUTO
Fundamental and applied biological sciences. Psychology
Gels
Mesocarp
Metabolism and Enzymology
METALLOPROTEINE
METALPROTEINAS
Microsomes
ORGANITE CELLULAIRE
ORGANULOS CITOPLASMATICOS
PEPTIDE
PEPTIDOS
PERSEA AMERICANA
Plant physiology and development
Proteins
Solvents
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Summary: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
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.89.4.1141