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Plant and Cell Physiology, 1985, Vol. 26, No. 3 389-395
© 1985

Article

Different Intracellular Localization of Two Cytochrome P-450 Systems, Ipomeamarone 15-Hydroxylase and Cinnamic Acid 4-Hydroxylase, in Sweet Potato Root Tissue Infected with Ceratocystis fimbriata

Masayuki Fujita1 and Tadashi Asahi2

Laboratory of Biochemistry, Faculty of Agriculture, Nagoya University Chikusa, Nagoya 464, Japan

2 To whom correspondence should be addressed

Ipomeamarone 15-hydroxylase activity was mainly recovered in the pellet fraction between centrifugations at 10,000 and 100,000×g from a crude extract of Ceratocystis fimbriata-infected sweet potato root tissue, whereas cinnamic acid 4-hydroxylase activity was found between centrifugations at 300 and 10,000×g. When particles in the crude extract were fractionated by sucrose density gradient centrifugation, the rough-surfaced microsomes were distributed over a wide density range from 1.09 to 1.14 g cm–3, judging from the distributions of protein, RNA and NADPH-cytochrome c reductase activity. Phosphorylcholine-glyceride transferase activity was only in the lighter half of the microsomal fraction (density: 1.09–1.11 g cm–3). Ipomeamarone 15-hydroxylase activity was found in heavier half of the microsomal fraction (density: 1.10–1.14 g cm–3). We propose that this tissue has two rough-surfaced endoplasmic reticulum species, only one of which carries phosphorylcholine-glyceride transferase, and that the cytochrome P-450 system is localized on the species lacking the enzyme. Cinnamic acid 4-hydroxylase activity was mainly found in a fraction that had densities of 1.17–1.19 g cm–3 and contained vesicular particles of various sizes.

1 Present address: Laboratory of Food Hygienics, Faculty of Agriculture, Kagawa University, Miki-cho, Kida-gun, Kagawa 761-07, Japan.

(Received September 6, 1984; Accepted December 27, 1984)
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