An improved purification method and a further characterization of the 33-kilodalton protein of spinach chloroplasts |
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Authors: | Tomohiko Kuwabara Norio Murata |
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Institution: | Department of Biology, University of Tokyo, Komaba, Meguro-ku, Tokyo 153 Japan |
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Abstract: | The 33-kDa protein was purified in a high yield from thylakoid membranes of spinach chloroplasts. The extinction coefficient and A1%1cm value at 276 nm of the protein were 22000 M?1·cm?1 and 6.8, respectively. The 33-kDa protein and a polypeptide appearing at 32 kDa in the SDS-polyacrylamide gel electrophoresis of thylakoid membranes were compared by peptide mapping after limited proteolysis. This indicates that the 32-kDa band is entirely due to the 33-kDa protein. The molar ratio of chlorophyll to the 33-kDa protein in the chloroplasts was estimated to be 300. This suggests that one photosynthetic unit possesses one or two molecules of the 33-kDa protein. |
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Keywords: | 33000-dalton protein Photosystem II (Spinach chloroplast) PS photosystem Mes 4-morpholine-ethanesulfonic acid |
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