Results 181 to 190 of about 29,742 (231)

Reprogramme the E. coli metabolism by engineering a functional carbon-fixation pathway. [PDF]

open access: yesJ Biol Eng
Chen Y   +8 more
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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
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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
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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
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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   +3 more
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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
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Ribulose bisphosphate carboxylase activity in halophilic Archaebacteria

Archives of Microbiology, 1990
Among the several strains of halobacteria grown heterotrophically, ribulose bisphosphate carboxylase activity was detected in those which accumulate poly (β-hydroxybutyrate), viz. Haloferax mediterranei, Haloferax volcanii and Halobacterium marismortui. In H.
Wijaya Altekar, Rema Rajagopalan
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Ribulose bisphosphate carboxylase/oxygenase from Thiocapsa roseopersicina

Archives of Microbiology, 1979
d-Ribulose-1,5-bisphosphate carboxylase/oxygenase has been purified 80-fold from malate-grown Thiocapsa roseopersicina by salting out the enzyme from the high-speed supernatant between 68–95% saturation with respect to (NH4)2SO4, gelfiltration through Sephadex G-100, and DEAE-cellulose chromatography followed by sedimentation into a 14–34% glycerol ...
K. Purohit   +2 more
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Carboxysomes and Ribulose Bisphosphate Carboxylase/Oxygenase

1988
Publisher Summary This chapter focuses on recent advances made in the knowledge of the occurrence, composition, properties, and possible functions of carboxysomes. It also discusses the rapidly expanding field of research on Ribulose 1, 5-bisphosphate carboxylase/oxygenase (RuBisCO) enzymes.
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