Polypeptide Composition of Envelope Membranes Isolated from Chloroplasts of C_3, C_4, and CAM Plants
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概要
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Chloroplast envelopes were isolated from chloroplasts purified from Spinacea oleracea L. (C_3), Panicum miliaceum L. (NAD-malic enzyme-type C_4), Digitaria sanguinalis (L.) Scop. (NADP-malic enzyme-type C_4). Kalanchoe daigremontiana Hamet et Perrier (constitutive CAM), and from Mesembryanthemum crystallinum L. (inducible CAM) performing either C_3 photosynthesis or Crassulacean acid metabolism (CAM). For each species, methods were developed to isolate chloroplast envelopes free of thylakoid contamination. The polypeptides of ribulose bisphosphate (RuBP) carboxylase which has been consistently reported in envelope preparations of spinach were not found in envelope preparations of C_4 mesophyll chloroplasts. Silver staining of envelope polypeptide resolved electrophoretically on sodium dodecylsulfate polyacrylamide gradient slab gels produced a more complex profile than did Coomassie staining which has previously been used with C_3 envelope preparations, even though silver reacted poorly with polypeptides corresponding to the subunits of RuBP carboxylase. All of the plants examined possessed a major polypeptide of 27 to 29 kilodaltons (kD) which was previously suggested to be the phosphate translocator in spinach. With C_3 M. crystallinum, the 29 kD polypeptide stained most intensely. After induction of CAM, a 32 kD polypeptide also stained intensely, giving a profile similar to that obtained with the constitutive CAM species. A 32 kD polypeptide was also prominent in C_4 envelope preparations, suggesting that a 32 kD polypeptide may be a translocator protein which is required in Crassulacean acid metabolism and C_4 photosynthesis, but not in C_3 photosynthesis.
- 日本植物生理学会の論文
著者
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Edwards Gerald
Department of Botany, Washington State University
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Edwards Gerald
Department Of Botany Washington State University
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Foster Joyce
Department Of Botany Washington State University:(present)united States Department Of Agriculture Ap
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