Results 121 to 130 of about 40,127 (172)

[Ribulose-bisphosphate carboxylase/oxygenase (author's transl)].

Postepy biochemii, 1979
openaire   +1 more source

Some of the next articles are maybe not open access.

Related searches:

Photoregulation of the biosynthesis of ribulose bisphosphate carboxylase

Development, 1984
ABSTRACT Chloroplast development in higher plants is light dependent, and is accompanied by the synthesis of chlorophyll and the accumulation of many chloroplast polypeptides. There is a 100-fold greater content of the photosynthetic enzyme, ribulose-l,5-bisphosphate carboxylase-oxygenase, in light-grown seedlings of Pisum sativum than ...
R J, Ellis, T F, Gallagher, G I, Jenkins, C R, Lennox   +3 more
openaire   +2 more sources

Modification of ribulose bisphosphate carboxylase by 2,3-butadione

Biochemical and Biophysical Research Communications, 1978
Abstract D-ribulose-1,5-bisphosphate carboxylases purified from barley or formate-grown Pseudomonas oxalaticus were inactivated by 2,3-butadione. Pseudo first-order inactivation depended on the presence of borate and was reduced by product 3-phosphoglycerate.
V B, Lawlis, B A, McFadden
openaire   +2 more sources

The lability of an intermediate of the ribulose bisphosphate carboxylase reaction

Archives of Biochemistry and Biophysics, 1983
Interruption of the catalytic cycle of ribulose-bisphosphate carboxylase by acid denaturation liberated an intermediate with a labile phosphate ester. Addition of fresh, buffered carboxylase enzyme to the acidified carboxylase reaction after 5 s inhibited phosphate release from the intermediate.
R M, Mulligan, N E, Tolbert
openaire   +2 more sources

Reutilization of Ribulose Bisphosphate Carboxylase

1978
Ribulose bisphosphate (RuBP) carboxylase is truly a multifunctional protein. Not only does it exhibit the well-known carboxylase and oxygenase activities, but also its high concentration and turnover characteristics in the leaf fit the classification of a storage protein.
R C, Huffaker, B L, Miller
openaire   +2 more sources

Stoichiometry in the assay of ribulose bisphosphate oxygenase and carboxylase

Analytical Biochemistry, 1982
Abstract Complete stoichiometry of the reaction catalyzed by ribulose 1,5-bisphosphate (RuBP) oxygenase from spinach and Rhodospirillum rubrum has been determined. Before initiation and after termination, RuBP has been measured either by release of equimolar orthophosphate at 25°C in the presence of 1 n NaOH or by complete carboxylation using 14CO2
K, Purohit, B A, McFadden, A, Saluja
openaire   +2 more sources

Chemosynthetic, Photosynthetic, and Cyanobacterial Ribulose Bisphosphate Carboxylase

1978
There are compelling reasons to believe that the initial atmosphere of the earth after its formation about 4.7 × 109 years ago was a reducing one consisting chiefly of methane, ammonia, water, and hydrogen (1). In the last two decades considerable research has been described in which numerous organic precursors of biopolymers have been synthesized ...
B A, McFadden, K, Purohit
openaire   +2 more sources

Catalytic Mutants of Ribulose Bisphosphate Carboxylase/Oxygenase

1978
Ribulose bisphosphate (RuBP) carboxylase/oxygenase, which may be the most abundant protein in nature, is recognized as the cardinal enzyme catalyzing carbon dioxide fixation yielding energy-rich photosynthate.
K, Andersen, W, King, R C, Valentine
openaire   +2 more sources