Separation and Characterization of Prolamellar Bodies and Prothylakoids from Squash Etioplasts
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概要
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Intact etioplasts of squash cotyledons, which had been prepared by Percoll density gradient centrifugation, were ruptured hypotonically in the presence of deoxyribonuclease I then fractionated into prolamellar bodies and prothylakoids by differential and Percoll density gradient centrifugations. This procedure provided a highly purified prolamellar body fraction that was composed mainly of a 36,000-dalton protein. This protein was identified as NADPH :protochlorophyllide oxidoreductase [Ikeuchi and Murakami (1982) Plant & Cell Physiol. 23: 1089] . The fraction also had a high content of protochlorophyllide that absorbed at 648 nm and its NADPH:protochlorophyllide oxidoreductase had high activity. When the fraction was illuminated, a chlorophyllide that absorbed at 684-685 nm formed. In contrast, the prothylakoid fraction, which showed high activity for the Ca^<2+>-dependent ATPase of coupling factor l, contained only a small amount of the 36.000-dalton protein and showed very low NADPH :protochlorophyllide oxidoreductase activity. The protochlorophyllide content of this fraction also was low, and the ratio of protochlorophyll to protochlorophyll(ide) high. The absorption peak in the prothylakoids was at 633-635 nm, and after a brief illumination a chlorophyllide that absorbed at 672-673 nm formed. These results indicate that the photoactive protochlorophyllide-NADPH-reductase complex in etioplasts is concentrated in the prolamellar body and that the physical state of protochlorophyll(ide) in the prolamellar body differs from that of the prothylakoid.
- 日本植物生理学会の論文
著者
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MURAKAMI Satoru
Department of Applied Mathematics Okayama University of Science
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Ikeuchi Masahiko
Department Of Biology College Of General Education University Of Tokyo
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