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. 1989 Apr;89(4):1141–1149. doi: 10.1104/pp.89.4.1141

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

Daniel P O'Keefe 1,2, Kenneth J Leto 1,2,1
PMCID: PMC1055988  PMID: 16666677

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Appleby C. A. Electron transport systems of Rhizobium japonicum. II. Rhizobium haemoglobin, cytochromes and oxidases in free-living (cultured) cells. Biochim Biophys Acta. 1969 Jan 14;172(1):88–105. doi: 10.1016/0005-2728(69)90094-2. [DOI] [PubMed] [Google Scholar]
  2. Benveniste I., Gabriac B., Durst F. Purification and characterization of the NADPH-cytochrome P-450 (cytochrome c) reductase from higher-plant microsomal fraction. Biochem J. 1986 Apr 15;235(2):365–373. doi: 10.1042/bj2350365. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. DUYSENS L. N. The flattening of the absorption spectrum of suspensions, as compared to that of solutions. Biochim Biophys Acta. 1956 Jan;19(1):1–12. doi: 10.1016/0006-3002(56)90380-8. [DOI] [PubMed] [Google Scholar]
  4. Dohn D. R., Krieger R. I. N-demethylation of p-chloro-N-methylaniline catalyzed by subcellular fractions from the avocado pear (Persea americana). Arch Biochem Biophys. 1984 Jun;231(2):416–423. doi: 10.1016/0003-9861(84)90405-3. [DOI] [PubMed] [Google Scholar]
  5. Funae Y., Imaoka S. Simultaneous purification of multiple forms of rat liver microsomal cytochrome P-450 by high-performance liquid chromatography. Biochim Biophys Acta. 1985 Oct 17;842(2-3):119–132. doi: 10.1016/0304-4165(85)90193-x. [DOI] [PubMed] [Google Scholar]
  6. Hasson E. P., West C. A. Properties of the System for the Mixed Function Oxidation of Kaurene and Kaurene Derivatives in Microsomes of the Immature Seed of Marah macrocarpus: Electron Transfer Components. Plant Physiol. 1976 Oct;58(4):479–484. doi: 10.1104/pp.58.4.479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Higashi K., Ikeuchi K., Karasaki Y., Obara M. Isolation of immunochemically distinct form of cytochrome P-450 from microsomes of tulip bulbs. Biochem Biophys Res Commun. 1983 Aug 30;115(1):46–52. doi: 10.1016/0006-291x(83)90966-x. [DOI] [PubMed] [Google Scholar]
  8. Huisman T. H. Separation of hemoglobins and hemoglobin chains by high-performance liquid chromatography. J Chromatogr. 1987 Jul 17;418:277–304. doi: 10.1016/0378-4347(87)80012-9. [DOI] [PubMed] [Google Scholar]
  9. Jefcoate C. R. Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy. Methods Enzymol. 1978;52:258–279. doi: 10.1016/s0076-6879(78)52029-6. [DOI] [PubMed] [Google Scholar]
  10. Jollie D. R., Sligar S. G., Schuler M. Purification and Characterization of Microsomal Cytochrome b(5) and NADH Cytochrome b(5) Reductase from Pisum sativum. Plant Physiol. 1987 Oct;85(2):457–462. doi: 10.1104/pp.85.2.457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. McPherson F. J., Markham A., Bridges J. W., Hartman G. C., Parke D. V. Effects of preincubation invitro with 3, 4-benzopyrene and phenobarbital on the drug-metabolism systems present in the microsomal and soluble fractions of the avocado pear (Persea americana). Biochem Soc Trans. 1975;3(2):283–285. doi: 10.1042/bst0030283. [DOI] [PubMed] [Google Scholar]
  13. OMURA T., SATO R. THE CARBON MONOXIDE-BINDING PIGMENT OF LIVER MICROSOMES. I. EVIDENCE FOR ITS HEMOPROTEIN NATURE. J Biol Chem. 1964 Jul;239:2370–2378. [PubMed] [Google Scholar]
  14. Poulos T. L., Finzel B. C., Gunsalus I. C., Wagner G. C., Kraut J. The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450. J Biol Chem. 1985 Dec 25;260(30):16122–16130. [PubMed] [Google Scholar]
  15. Rifkind A. B., Petschke T. p-Chloro-N-methylaniline demethylase activity in liver and extrahepatic tissues of the human fetus and in chick embryo liver. J Pharmacol Exp Ther. 1981 Jun;217(3):572–578. [PubMed] [Google Scholar]
  16. Rivier J., McClintock R. Reversed-phase high-performance liquid chromatography of insulins from different species. J Chromatogr. 1983 Sep 23;268(1):112–119. doi: 10.1016/s0021-9673(01)95395-6. [DOI] [PubMed] [Google Scholar]
  17. Robb R. J., Kutny R. M., Chowdhry V. Purification and partial sequence analysis of human T-cell growth factor. Proc Natl Acad Sci U S A. 1983 Oct;80(19):5990–5994. doi: 10.1073/pnas.80.19.5990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Romesser J. A., O'Keefe D. P. Induction of cytochrome P-450-dependent sulfonylurea metabolism in Streptomyces griseolus. Biochem Biophys Res Commun. 1986 Oct 30;140(2):650–659. doi: 10.1016/0006-291x(86)90781-3. [DOI] [PubMed] [Google Scholar]
  19. Sabatini D. D., Kreibich G., Morimoto T., Adesnik M. Mechanisms for the incorporation of proteins in membranes and organelles. J Cell Biol. 1982 Jan;92(1):1–22. doi: 10.1083/jcb.92.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Yuan P. M., Ryan D. E., Levin W., Shively J. E. Identification and localization of amino acid substitutions between two phenobarbital-inducible rat hepatic microsomal cytochromes P-450 by micro sequence analyses. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1169–1173. doi: 10.1073/pnas.80.5.1169. [DOI] [PMC free article] [PubMed] [Google Scholar]

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