Results 231 to 240 of about 28,045 (260)
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FEMS Microbiology Letters, 1997
Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) catalyzes the key reaction of the Calvin reductive pentose phosphate cycle and as such is responsible for life as we know it. This enzyme has been intensively studied for decades.
G. Watson, F. Tabita
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Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) catalyzes the key reaction of the Calvin reductive pentose phosphate cycle and as such is responsible for life as we know it. This enzyme has been intensively studied for decades.
G. Watson, F. Tabita
semanticscholar +1 more source
Biochemical and Biophysical Research Communications, 1986
RuBPCase from peas showed Ribose-5-phosphate and Ribulose-5-phosphate dependent CO2 fixation when purified on sucrose gradients or by conventional methods. If purification was done in the presence of 20 mM MgCl2 and 20-25 mM NaHCO3 RuBPCase showed higher Ribose-5-phosphate and Ribulose-5-phosphate dependent CO2 fixation rates.
Jayashree K. Sainis, Gary C. Harris
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RuBPCase from peas showed Ribose-5-phosphate and Ribulose-5-phosphate dependent CO2 fixation when purified on sucrose gradients or by conventional methods. If purification was done in the presence of 20 mM MgCl2 and 20-25 mM NaHCO3 RuBPCase showed higher Ribose-5-phosphate and Ribulose-5-phosphate dependent CO2 fixation rates.
Jayashree K. Sainis, Gary C. Harris
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Ribulose-1,5-bisphosphate carboxylase/oxygenase from parsley
Biochemical and Biophysical Research Communications, 1978Abstract Ribulose-1,5-bisphosphate carboxylase/oxygenase from parsley leaves was purified by Sepharose 6B gel filtration at pH 8.3 as a single, colorless peak containing both activities. Approximately 0.2 g atom copper per mole enzyme was detected by atomic absorption spectroscopy, but this copper was not detectable by EPR spectrometry.
Stephen D. McCurry +4 more
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Biochemistry, 1978
Ribulose-1,5-bisphosphate carboxylase catalyzes the conversion of D ribulose 1,5-bisphosphate and CO2 to 3-phospho-D-glycerate, with retention of the oxygen atoms at both C-2 and C-3 of the substrate. This observation is consistent with mechanistic pathways involving an enediol intermediate and eliminates suggested mechanisms that involve covalent ...
Jeremy R. Knowles, Julia M. Sue
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Ribulose-1,5-bisphosphate carboxylase catalyzes the conversion of D ribulose 1,5-bisphosphate and CO2 to 3-phospho-D-glycerate, with retention of the oxygen atoms at both C-2 and C-3 of the substrate. This observation is consistent with mechanistic pathways involving an enediol intermediate and eliminates suggested mechanisms that involve covalent ...
Jeremy R. Knowles, Julia M. Sue
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Separation of Ribulose 1,5-Bisphosphate Carboxylase and Oxygenase Activities
1978Recently it was shown that RuBP carboxylase and RuBP oxygenase activities were separated when the enzymes were prepared at a higher pH than normally used (1). Recent reports (2, 3), as well as some characteristics of the enzyme found earlier (4), e.g., the different behaviors of the two activities upon storage, suggest that two different enzymes are ...
Carl-Ivan Brändén, Rolf Brändén
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Biochemistry, 1982
The reaction of [3-3H]ribulose 1,5-bisphosphate and CO2 with ribulose-1,5-bisphosphate carboxylase has been investigated in order to provide information about the early steps of the enzyme-catalyzed reaction. The specific radioactivity of ribulose 1,5-bisphosphate reisolated after partial reaction rises as the reaction proceeds, demonstrating that the ...
Jeremy R. Knowles, Julia M. Sue
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The reaction of [3-3H]ribulose 1,5-bisphosphate and CO2 with ribulose-1,5-bisphosphate carboxylase has been investigated in order to provide information about the early steps of the enzyme-catalyzed reaction. The specific radioactivity of ribulose 1,5-bisphosphate reisolated after partial reaction rises as the reaction proceeds, demonstrating that the ...
Jeremy R. Knowles, Julia M. Sue
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, 1989
A mathematical framework was developed to analyse rate limitation of non-steady-state photosynthesis following an increase in photon flux density (PFD). This analysis was employed to resolve an exponential phase of the photosynthetic response of Spinacia
I. E. Woodrow, K. Mott
semanticscholar +1 more source
A mathematical framework was developed to analyse rate limitation of non-steady-state photosynthesis following an increase in photon flux density (PFD). This analysis was employed to resolve an exponential phase of the photosynthetic response of Spinacia
I. E. Woodrow, K. Mott
semanticscholar +1 more source
Ribulose-1,5-Bisphosphate Carboxylase
1979Biochemical studies on leaf proteins carried out by Wildman and Bonner (1947) revealed the presence of a major protein component having a large molecular size (18s) which was designated as fraction-1-protein. The ubiquitous distribution of this protein in green plant leaves and green algae, as determined by analytical ultracentrifugation and ...
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Archives of Biochemistry and Biophysics, 1991
The large subunit (L) of ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) from Synechococcus PCC 6301 was expressed in Escherichia coli, purified as the octamer L8, and analyzed for its ability to tightly bind the transition state analog, 2-carboxyarabinitol 1,5-bisphosphate (CABP). [14C]CABP remained tightly bound to L8 after challenging with
Hans J. Bohnert +2 more
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The large subunit (L) of ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) from Synechococcus PCC 6301 was expressed in Escherichia coli, purified as the octamer L8, and analyzed for its ability to tightly bind the transition state analog, 2-carboxyarabinitol 1,5-bisphosphate (CABP). [14C]CABP remained tightly bound to L8 after challenging with
Hans J. Bohnert +2 more
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Active Site of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase
1978The properties, distribution, biogenesis, function, and regulation of ribulose bisphosphate carboxylase/oxygenase, as described elsewhere in this Symposium, are mainly integrated around the mechanism of action of the carboxylase and oxygenase reactions.
Stephen D. McCurry +3 more
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