Results 211 to 220 of about 25,095 (239)
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Applied Microbiology and Biotechnology, 2017
D-Ribulose-5-phosphate-3-epimerase (RPE) and 6-phosphofructokinase (PFK) catalyse two reactions in the ribulose monophosphate (RuMP) cycle in Bacillus methanolicus. The B. methanolicus wild-type strain MGA3 possesses two putative rpe and pfk genes encoded on plasmid pBM19 (rpe1-MGA3 and pfk1-MGA3) and on the chromosome (rpe2-MGA3 and pfk2-MGA3).
Simone Balzer, Le +4 more
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D-Ribulose-5-phosphate-3-epimerase (RPE) and 6-phosphofructokinase (PFK) catalyse two reactions in the ribulose monophosphate (RuMP) cycle in Bacillus methanolicus. The B. methanolicus wild-type strain MGA3 possesses two putative rpe and pfk genes encoded on plasmid pBM19 (rpe1-MGA3 and pfk1-MGA3) and on the chromosome (rpe2-MGA3 and pfk2-MGA3).
Simone Balzer, Le +4 more
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1975
Publisher Summary D-Ribulose may be prepared by chemical or enzymic methods. Normally, enzymic means of preparation yield D-ribulose possessing higher biological activity as determined by measuring the percentage of sugar utilized by a specific enzyme.
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Publisher Summary D-Ribulose may be prepared by chemical or enzymic methods. Normally, enzymic means of preparation yield D-ribulose possessing higher biological activity as determined by measuring the percentage of sugar utilized by a specific enzyme.
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Biochemical and Biophysical Research Communications, 1973
Abstract Ribulose-1,5-diphosphate car☐ylase from the photosynthetic bacterium Chromatium catalyses the oxidative formation of phosphoglycolate and 3-phosphoglycerate from ribulose-1,5-diphosphate at an alkaline pH (9.3) in an atmosphere of oxygen.
T, Takabe, T, Akazawa
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Abstract Ribulose-1,5-diphosphate car☐ylase from the photosynthetic bacterium Chromatium catalyses the oxidative formation of phosphoglycolate and 3-phosphoglycerate from ribulose-1,5-diphosphate at an alkaline pH (9.3) in an atmosphere of oxygen.
T, Takabe, T, Akazawa
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Ribulose-Peptide in Human Semen: I. Isolation
Archives of Andrology, 1978A substance apparently related to a compound consisting of phospho-peptide and ribulose-peptide in the yolk of chick embryos was isolated from acid soluble fractions of human semen by means of Dowex 1 (OH) form column chromatography. The treated precipitate of human semen was examined with an analytical ultracentrifuge by means of synthetic boundary ...
H, Amano +3 more
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Ribulose 1,5-diphosphate carboxylase and Chlorobium thiosulfatophilum
Archives of Microbiology, 19761. Cell-free extracts of the photosynthetic bacterium Cholorobium thiosulfatophilum, strains 8327 and Tassajara, were assayed for ribulose 1,5-diphosphate (RuDP) carboxylase and phosphoribulokinase--the two enzymes peculiar to the reductive pentose phosphate cycle. 2. RuDP carboxylase was consistently absent in strain 8327.
B B, Buchanan, R, Sirevåg
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Aerobic dissimilation of d-ribulose by yeasts
Antonie van Leeuwenhoek, 1970Aerobic dissimilation ofd-ribulose by various genera and species of yeasts was examined. Most strains tested utilizedd-ribulose fairly well, andd-arabitol was accumulated in the fermented broth but ribitol was not found. Torulopsis famata ATCC 20214,T.mannitofaciens CBS 5981 andT.versatilis CBS 1752 producedd-arabitol with a yield of 26 to 67% of the ...
T, Suzuki, H, Onishi
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Bicarbonate stabilization of ribulose 1,5-diphosphate carboxylase
Biochemistry, 1975The carboxylase and oxygenase activities of purified soybean ribulose 1,5-di-P carboxylase (EC4.1.1.39) were unstable when reactions were initiated with enzyme. Time courses of carboxylase and oxygenase activities were curvilinear, approximating hyperbolas. Double reciprocal plots of amount of CO2 incorporated and P-glycolate produced vs.
W A, Laing, W L, Ogren, R H, Hageman
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Carboxysomes and Ribulose Bisphosphate Carboxylase/Oxygenase
1988Publisher 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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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.
S D, McCurry +4 more
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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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