High specific activity ribulose 1,5-bisphosphate carboxylase-oxygenase from Nicotiana tabacum |
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| Authors: | James T Bahr Sarjit Johal Malcolm Capel Don P Bourque |
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| Institution: | (1) Department of Biochemistry, University of Arizona, 85721 Tucson, AR, USA;(2) Department of Nutrition and Food Science, University of Arizona, 85721 Tucson, AR, USA;(3) Present address: Rhone-Poulenc Chemical Co., P.O. Box 125, 08852 Monmouth Junction, NJ, USA;(4) Present address: Department of Agricultural Biochemistry, University of Nebraska, 68583 Lincoln, NE, USA;(5) Department of Biochemistry, University of Arizona, 309 Agricultural Sciences Bldg., 85721 Tucson, AR, USA |
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| Abstract: | Ribulose 1,5-bisphosphate carboxylase (EC.4.1.1.39) has been obtained from Nicotiana tabacum leaf homogenates with specific activites from 0.5 to 0.8 µmol CO2 fixed (mg protein min)-1. These activities are reconciled with much lower, previously reported activities. The results suggest that if the tobacco enzyme is assayed under optimum conditions there is little difference in the intrinsic specific activities of tobacco and spinach ribulose 1,5-bisphosphate carboxylase. Several factors affecting activity measurements were examined. |
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| Keywords: | Ru-P2 carboxylase long-term assay short-term assay specific activity tobacco |
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