Results 221 to 230 of about 28,959 (255)

Inhibition of ribulose-1,5-bisphosphate carboxylase/oxygenase by ribulose-1,5-bisphosphate epimerization and degradation products

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 ...
C, Paech, J, Pierce, S D, McCurry, N E, Tolbert   +3 more
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The Activation of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase

1978
A 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).
G H, Lorimer, M R, Badger, H W, Heldt
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Ribulose-1,5-Bisphosphate Carboxylase

1979
Biochemical 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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d-ribulose-1,5-bisphosphate carboxylase in Chlorobium thiosulfatophilum Tassajara

Biochimica et Biophysica Acta (BBA) - Enzymology, 1974
Abstract d -Ribulose-1,5-bisphosphate carboxylase (3-phospho- d -glycerate carboxy-lyase (dimerizing), EC 4.1.1.39) was readily detected in extracts of Chlorobium thiosulfatophilium Tassajara after transatlantic air delivery. The enzyme, which was moderately unstable, had a specific activity of 7 nmoles CO 2 fixed/min per mg protein when assayed ...
F R, Tabita, B A, McFadden, N, Pfennig
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Active Site of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase

1978
The 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.
C, Paech, S D, McCurry, J, Pierce, N E, Tolbert   +3 more
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Subunit arrangement of spinach ribulose 1,5-bisphosphate carboxylase/oxygenase

Planta, 1985
The structure of spinach ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) has been investigated by tilted-view electron microscopy of negatively stained monolayer crystals and image processing. The structure determined consists of a cylinder of octagonal cross-section with a large central hole.
J A, Barcena, P J, Shaw
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Ribulose 1,5-bisphosphate carboxylase: fate of the tritium label in [3-3H]ribulose 1,5-bisphosphate during the enzyme-catalyzed reaction

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 ...
J M, Sue, J R, Knowles
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Separation of Ribulose 1,5-Bisphosphate Carboxylase and Oxygenase Activities

1978
Recently 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 ...
R, Brändén, C I, Brändén
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Regulation of Ribulose 1,5-Bisphosphate Carboxylase in the Chloroplast

1978
Carbon 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).
R G, Jensen, R C, Sicher, J T, Bahr
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Isolation of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase from Leaves

2010
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a multifunctional enzyme that catalyzes the fixation of CO2 and O2 in photosynthesis and photorespiration, respectively. As the rate-limiting step in photosynthesis, improving the catalytic properties of Rubisco has long been viewed as a viable strategy for increasing plant productivity ...
Carmo-Silva, A. Elizabete, Barta, Csengele, Salvucci, Michael E.   +2 more
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