Senescence-Induced, Thylakoid-Bound Diisopropylfluorophosphate-Binding Protein in Spinach
書誌事項
- タイトル別名
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- Induction Pattern, Localization, and Some Properties
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説明
Changes in diisopropylfluorophosphate (DFP)-binding proteins during development and senescence of spinach (Spinacia oleracea) leaves were followed using [(3)H]DFP and sodium dodecylsulfate-polyacrylamide gel electrophoresis-fluorography. Experiments using a series of aging stages of leaves attached to plants and ones with detached leaves stored in the dark both showed that a protein of 38 kilodaltons was the only major DFP-binding protein in the membrane fraction and that its DFP-binding increased markedly as senescence proceeded, corresponding with the degradation of leaf protein. DFP binding to the 38-kilodalton protein was not affected by membrane solubilization with Triton X-100, and gradually decreased upon preservation of the membranes. The DFP binding was inhibited completely by phenylmethane-sulfonyl fluoride and slightly by p-chloromercuribenzoic acid, suggesting a serine protease-like character of the protein and a possible contribution of SH residues to the binding. Both differential and Percoll-gradient centrifugation indicated that the 38-kilodalton protein was localized in thylakoid membranes. The sedimentation behavior of the detergent-solubilized protein indicated that it belongs to a complex different from photosystem I, photosystem II, or coupling factor 1 of the ATP-synthesizing complex.
収録刊行物
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- Plant Physiology
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Plant Physiology 90 338-344, 1989-05-01
Oxford University Press (OUP)