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- Publisher
- Springer Journals
- Copyright
- Copyright © 1986 by Springer-Verlag
- Subject
- Life Sciences; Biotechnology; Biochemistry, general; Cell Biology; Ecology; Microbial Ecology; Microbiology
- ISSN
- 0302-8933
- eISSN
- 1432-072X
- DOI
- 10.1007/BF00454961
- Publisher site
- See Article on Publisher Site
Abstract
203 144 144 1 1 Anne E. Desjardins Hans D. VanEtten Department of Plant Pathology Cornell University 14853-0331 Ithaca NY USA Northern Regional Research Center USDA 1815 N. University Street 61604 Peoria IL USA Abstract The plant pathogen Nectria haematococca can demethylate pisatin, a phytoalexin from pea. Demethylation is apparently necessary for virulence on pea and is catalyzed by a microsomal cytochrome P-450 monooxygenase system. The cytochrome P-450 and NADPH-cytochrome P-450 reductase of this system were solubilized with sodium cholate and partially purified by chromatography on blue A-agarose and ω-aminohexyl-agarose. The reductase was further purified by chromatography on 2′,5′-ADP-agarose to a specific activity of about 16 μmoles cytochrome c reduced per min per mg protein. Upon sodium dodecyl sulfatepolyacrylamide gel electrophoresis, the reductase fraction contained one major band of molecular weight 84,000. The partially purified cytochrome P-450 fraction contained a number of minor bands and three major bands of molecular weights 52,000, 56,000 and 58,000. This fraction lost all demethylase activity during concentration after ω-aminohexyl-agarose chromatography, so it could not be purified further. The purified reductase could reconstitute demethylase activity of cytochrome P-450 fractions and appeared to be rate-limiting for demethylase activity in microsomal extracts.
Journal
Archives of Microbiology – Springer Journals
Published: Feb 1, 1986