Abstract
Ribulose-1, 5-diphosphate carboxylase isolated from autotrophically grown cells of the green algae, Chlorella ellipsoidea, was partially purified. The nature of the enzyme closely resembles the spinach leaf enzyme in its elution patterns on Sephadex gel filtration and DEAE-cellulose column chromatography, migration on starch gel electrophoresis, and the immunological specificity. Chlorella RuDP carboxylase exhibits essentially identical kinetic parameters of the regulatory enzyme with those of spinach enzyme: (a) homotropic effect of NaHCO 3, (b) allosteric activating effect of Mg 2+ with respect to NaHCO 3, and (c) shift of optimum pH by elevating the Mg 2+ concentrations.
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