Comparison of the specific activity of ribulose-1,5-bis-phosphate carboxylase-oxygenase from some C3 and C4 plants |
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Authors: | Eevi Rintamäki Alfred J Keys Martin A J Parry |
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Institution: | Dept of Biology, Univ, of Turku, SF-20500 Turku, Finland;Rothamsted Experimental Station, Harpenden, Herts AL5 2JQ, England. |
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Abstract: | The specific activity of ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco, EC 4.1.1.39) was measured from the crude extracts of five C3 plants consisting of wheat ( Triticum aestivum L. cv. Maris Mink), spinach ( Spinacia oleracea L.), pea ( Pisum sativum L. cv. Greenfeast), pumpkin ( Cucurbita pepo L. cv. Jättiläismeloni) and Ceratodon purpureus (Hedw.) Brid., and two C4 plants, maize ( Zea mays L. ETA F1) and sugar sorghum Sorghum saccharatum (L. emend, L.) Moench]. The amount of Rubisco in the crude extracts was estimated by polyacrylamide gel electro-phoresis with the Coomassie Brilliant Blue staining procedure. The amounts of the dye bound to the purified Rubisco of different higher plants were similar. The method gave a linear response for both purified enzyme and crude extracts, and the results agreed with those observed by immunochemical methods. The addition of positive effectors such as inorganic phosphate was necessary to obtain maximal activity in the crude extracts of all the studied plants except in that of maize. No significant differences in the specific carboxylase activity at 25°C were found between the C3 and C4 plants. |
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Keywords: | C3 plants C4 plants Ceratodon purpureus Cucurbita pepo inorganicphosphate Pisum sativum polyacrylamide gel electrophoresis ribulose-1 5-bisphosphate carboxylase-oxygenase Rubisco Sorghum saccharatum specific activity Spinacia oleracea Triticum aestivum Zea mays |
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