Abstract
Higher plant-type ribulosebisphoshate carboxylase from Chromatium vinosum formed a stable, nonexchangeable complex with activator 14CO2 in the presence of Mg2+ and 2-carboxyarabinitol bisphosphate, an analog of the proposed transition-state intermediate. The response of the procaryotic enzyme to this analog was indistinguishable from that of the higher-plant carboxylase, which should permit comparative analysis of the activator site amino acid sequence in the two proteins.
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Selected References
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