Solubilization of ribulose-1,5-bisphosphate carboxylase from the membrane fraction of pea leaves |
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Authors: | Amane Makino Barry Osmond |
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Institution: | (1) Department of Botany, Duke University, 27706 Durham, North Carolina, USA;(2) Present address: Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University, Tsutsumidori-Amamiyamachi, 981 Sendai, Japan;(3) Present address: Research School of Biological Sciences, Australian National University, Box 475, 2601 Canberra, Australia |
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Abstract: | The solubilization of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from the membrane fraction was studied in whole leaf extracts and chloroplasts from pea. The amount of membrane-bound Rubisco was dependent on the pH of the chloroplastic lysate buffer. Maximum binding was found at pH 8.0, with about 8% of total leaf Rubisco being bound. The binding of Rubisco to the membranes was strong, and it was not released by repeated washing with hypotonic buffer or by changing ionic strength. Detergents such as Triton X-100, Tween 20, deoxycholate and dodecylsulfate were effective in solubilizing the membrane-bound Rubisco. Triton X-100 was most effective in the range of 0.04% to 0.2% and it solubilized Rubisco from the membrane without any decrease in enzyme activity.Abbreviations BSA
bovine serum albumin
- CABP
carboxyarabinitol-1,5-bisphosphate
- DTT
dithiothreitol
- LDS
lithium dodecylsulfate
- LHC
light-harvesting chlorophyll protein complex
- RuBP
ribulose-1,5-bisphosphate
- Rubisco
RuBP carboxylase/oxygenase
- SDS
sodium dodecylsulfate
- SDS-PAGE
SDS-polyacrylamide gel electrophoresis |
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Keywords: | chloroplasts Pisum sativum L Rubisco thylakoids Triton X-100 |
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