Presence of two subunit types in ribulose-1,5-bisphosphate carboxylase from blue-green algae. |
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Authors: | T Takabe M Nishimura T Akazawa |
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Institution: | Research Institute for Biochemical Reggulation Nagoya University, School of Agriculture Chikusa, Nagoya 464 Japan |
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Abstract: | Ribulose-1,5-bisphosphate car?ylase (E.C. 4.1.1.39) from 2 blue-green algae, Plectonema boryanum and Anabaena variabilis, was isolated by sucrose density gradient centrifugation. Both enzymes had a sedimentation value of about 18s, similar to that of Chromatium enzyme. The presence of two subunits (A, B) in the algal enzyme was demonstrated by Nadodecyl sulfate polyacrylamide gel electrophoresis. The molecular weight of the two subunits was determined: for Plectonema A, 5.4 × 104 and B, 1.3 × 104 and Anabaena A, 5.2 × 104 and B, 1.3 × 104, respectively. The car?ylase reaction catalysed by the algal enzyme was similar to the higher plant enzyme in exhibiting the Mg2+-effect, the optimal pH shifting from alkaline to neutral by elevating the concentration of Mg2+ in the assay mixture. The rabbit antisera developed against the spinach ribulose-1,5-bisphosphate car?ylase and its catalytic oligomer exhibited significant inhibitory effects on the car?ylation reaction catalysed by the algal enzyme. |
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Keywords: | DTT dithiothreitol RuDP ribulose-1 5-bisphosphate |
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