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ribulose diphosphate carboxylase/spinacia oleracea
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14 results
Ribulose Diphosphate Carboxylase from Freshly Ruptured Spinach Chloroplasts Having an in Vivo Km[CO(2)].
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The properties of a form of ribulose diphosphate carboxylase having a high affinity for CO(2) have been studied. Its apparent Km(HCO(3) (-)) of 0.5 to 0.8 mm (pH 7.8) and calculated Km(CO(2)) of 11 to 18 mum are comparable to the values exhibited by intact chloroplasts during photosynthesis. This
Factors affecting interconversion between kinetic forms of ribulose diphosphate carboxylase-oxygenase from spinach.
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Effects of CO2, O2 and temperature on a high-affinity form of ribulose diphosphate carboxylase-oxygenase from spinach.
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Urea denaturation of spinach leaf ribulose diphosphate carboxylase.
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Spinach ribulose diphosphate carboxylase. I. Purification and properties of the enzyme.
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The presence of tightly bound copper in ribulose diphosphate carboxylase from spinach.
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The distribution of carbonic anhydrase and ribulose diphosphate carboxylase in maize leaves.
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Extraction of maize (Zea mays) leaves by progressive grinding under suitably protective conditions yields total carbonic anhydrase activities (4800 units per milligram chlorophyll) comparable to the activity in spinach (Spinacia oleracea) leaves. The total ribulose diphosphate carboxylase activity
Compositional characteristics of a chloroform/methanol soluble protein fraction from spinach chloroplast membranes.
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Extraction of an aqueous suspension of spinach chloroplast lamellae with a chloroform/methanol mixture leads to solubilization of about 1/3 of the total membrane protein. Amino acid analysis of the chloroform/methanol-soluble protein shows that this fraction is largely enriched in the hydrophobic
Ribulose diphosphate carboxylase/oxygenase. III. Isolation and properties.
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Similarities in properties of ribulose diphosphate carboxylase and oxygenase activities further substantiate the hypothesis that the same protein catalyzes both reactions. The Km (ribulose diphosphate) is 0.33 mM for the ribulose diphosphate oxygenase, when assayed in air with an oxygen electrode.
Uptake of bicarbonate ion in darkness by isolated chloroplast envelope membranes and intact chloroplasts of spinach.
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Bicarbonate uptake by isolated chloroplast envelope membranes and intact chloroplasts of spinach (Spinacia oleracea L. var. Viroflay) in darkness exhibited a similar dependency upon temperature, pH, time, and concentrations of isolated or attached envelope membranes. This similarity in uptake
Chloroplast Integrity and ATP-Dependent CO(2) Fixation in Spinacia oleracea.
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Washed whole chloroplasts of Spinacia oleracea isolated and assayed in a tris (hydroxymethyl aminomethane)-HCl buffered sucrose solution exhibited low dark CO(2) fixing activity, whereas washed whole chloroplasts isolated in the same buffer but assayed in that buffer without sucrose exhibited much
Localization and properties of ribulose diphosphate carboxylase from castor bean endosperm.
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A substantial portion of the ribulose 1,5-diphosphate carboxylase activity in the endosperm of germinating castor beans (Ricinus communis var. Hale) is recovered in the proplastid fraction. The partially purified enzyme shows homology with the enzyme from spinach (Spinacia oleracea) leaves, as
Ribulose Diphosphate Carboxylase from Autotrophic Euglena gracilis.
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Ribulose 1,5-diphosphate carboxylase (RUDPcase) from autotrophically grown Euglena gracilis was purified to homogeneity as measured by analytical ultracentrifugation, polyacrylamide gel electrophoresis, and immunoprecipitation reactions. The enzyme represented about 9% of total protein and 24% of
Synthesis of Proteins by Isolated Euglena gracilis Chloroplasts.
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Intact Euglena gracilis chloroplasts, which had been purified on gradients of silica sol, incorporated [(35)S]methionine or [(3)H]leucine into soluble and membrane-bound products, using light as the only source of energy. The chloroplasts were osmotically shocked, fractionated on discontinuous
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