Results 221 to 230 of about 28,045 (260)
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Biochemistry, 1976
Ribulose-1,5-bisphosphate carboxylase was activated by incubation with CO2 and Mg2++, and inactivated upon removal of CO2 and Mg2+ by gel filtration. The activation process involved CO2 rather than HCO3-. The activity of the enzyme was dependent upon the
G. Lorimer, M. Badger, T. Andrews
semanticscholar +1 more source
Ribulose-1,5-bisphosphate carboxylase was activated by incubation with CO2 and Mg2++, and inactivated upon removal of CO2 and Mg2+ by gel filtration. The activation process involved CO2 rather than HCO3-. The activity of the enzyme was dependent upon the
G. Lorimer, M. Badger, T. Andrews
semanticscholar +1 more source
Ribulose 1,5-bisphosphate carboxylase and phosphoribulokinase in Prochloron
Planta, 1983Cell-free extracts of Prochloron didemni were assayed for ribulose 1,5-bisphosphate (RuBP) carboxylase (EC 4.1.1.39) and phosphoribulokinase (EC 2.7.1.19), two key enzymes in the reductive pentose-phosphate cycle. In an RuBP-dependent reaction, the production of two molecules of 3-phosphoglycerate per molecule of CO2 fixed was shown ...
Bruce A. McFadden, Mark A. Berhow
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Regulation of Ribulose 1,5-Bisphosphate Carboxylase in the Chloroplast
1978Carbon dioxide is incorporated by the action of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBP carboxylase) during photosynthesis. Curves relating photosynthesis rates to illuminance for many species, especially C3 plants, show that the photosynthesis rate approaches a limiting value asymptotically at high radiation (1, 2).
Richard G. Jensen +2 more
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Biochemistry, 1982
The primary deuterium kinetic isotope effect for the reaction of [3-2H]ribulose 1,5-bisphosphate with CO2 in the reaction catalyzed by ribulose-1,5-bisphosphate carboxylase has been determined. By use of highly purified substrates containing less than 0.13% of the C-3 epimer xylulose 1,5-bisphosphate (this material is known to be a potent competitive ...
Jeremy R. Knowles, Julia M. Sue
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The primary deuterium kinetic isotope effect for the reaction of [3-2H]ribulose 1,5-bisphosphate with CO2 in the reaction catalyzed by ribulose-1,5-bisphosphate carboxylase has been determined. By use of highly purified substrates containing less than 0.13% of the C-3 epimer xylulose 1,5-bisphosphate (this material is known to be a potent competitive ...
Jeremy R. Knowles, Julia M. Sue
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Regulation of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase Activity
, 1992INTRODUCTION . . . . . . ... .... .. .... ..... . ... 416 BIOCHEMICAL BASIS FOR INTRINSIC CHANGES IN ACTIVITy. .. .. . . .. . . . . . . . . . . 416 Influence of Sugar Phosphates . .. . . . . . . . . . . . . ... ... ... .. . ... . . . . . . . ...
A. Portis
semanticscholar +1 more source
Biochemical and Biophysical Research Communications - BBRC, 1997
Strongly carboxylase-specific ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) was found in Galdieria partita and Cyanidium caldarium (Cyanidiophyceae).
K. Uemura +3 more
semanticscholar +1 more source
Strongly carboxylase-specific ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) was found in Galdieria partita and Cyanidium caldarium (Cyanidiophyceae).
K. Uemura +3 more
semanticscholar +1 more source
Biochemical and Biophysical Research Communications, 1978
Abstract Xylulose-1,5-bisphosphate in preparations of ribulose-1,5-bisphosphate (ribulose-P2) arises from non-enzymic epimerization and inhibits the enzyme. Another inhibitor, a diketo degradation product from ribulose-P2, is also present. Both compounds simulate the substrate inhibition of ribulose-P2 carboxylase/oxygenase previously reported for ...
Christian Paech +3 more
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Abstract Xylulose-1,5-bisphosphate in preparations of ribulose-1,5-bisphosphate (ribulose-P2) arises from non-enzymic epimerization and inhibits the enzyme. Another inhibitor, a diketo degradation product from ribulose-P2, is also present. Both compounds simulate the substrate inhibition of ribulose-P2 carboxylase/oxygenase previously reported for ...
Christian Paech +3 more
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The Activation of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase
1978A long-standing and continuing problem concerning ribulose bisphosphate carboxylase/oxygenase is the discrepancy between its activity in vivo and in vitro (1, 2). The apparently low affinity of the enzyme for CO2 was one of the better reasons Warburg had for dismissing the C3 photosynthetic carbon reduction cycle (3).
Murray R. Badger +2 more
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Ribulose-1,5-bisphosphate carboxylase as a nuclear and chloroplast marker
Theoretical and Applied Genetics, 1978The data on the primary structure of ribulose-1,5-bisphosphate carboxylase/oxygenase are reviewed. Examples of their use as markers and in the elucidation of the evolution, adaptation and function of this key enzyme are given.
Anthony A. Holder +2 more
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Small subunit contacts in ribulose-1,5-bisphosphate carboxylase
Biochemistry, 1978The arrangement of subunits of ribulosebisphosphate carboxylase in solution has been studied by exposing the enzyme to the cross-linking agents tetranitromethane, dimethyl suberimidate, and dimethyl adipimidate, and the cleavable cross-linking agent, methyl 4-mercaptobutyrimidate followed by gel electrophoresis in the presence of dodecyl sulfate.
Linda Rueckert +4 more
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