Results 171 to 180 of about 10,894 (204)
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Complexes of muscle aldolase in equilibrium with fructose 1,6-bisphosphate
Biochemistry, 1985Minimum values for the content of covalent intermediates in the equilibria of muscle aldolase with its cleavable substrates have been determined by acid denaturation/precipitation. Ribulose 1,5-bisphosphate, a nonsubstrate that binds well to aldolase in the native state, does not form a covalent complex that is acid precipitable.
I A, Rose, J V, Warms
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Fructose-1,6-bisphosphate aldolase fromVibrio marinus, a psychrophilic marine bacterium
Zeitschrift für allgemeine Mikrobiologie, 1979AbstractFructose‐1,6‐bisphosphate aldolase (Fru‐P2A) from a psychrophilic marine bacterium was found to be Class II aldolase based on activation by K+, activation by divalent cations, inactivation by EDTA, low molecular weight, and similar values for Km, Vmax, and ARRHENIUS activation energy.
L P, Jones, R Y, Morita, R R, Becker
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Biochemistry (Moscow), 2010
The gene fba from the thermotolerant obligate methanotroph Methylococcus capsulatus Bath was cloned and expressed in Escherichia coli BL21(DE3). The fructose-1,6-bisphosphate aldolase (FBA) carrying six His on the C-end was purified by affinity metal chelating chromatography. The Mc.
O N, Rozova +4 more
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The gene fba from the thermotolerant obligate methanotroph Methylococcus capsulatus Bath was cloned and expressed in Escherichia coli BL21(DE3). The fructose-1,6-bisphosphate aldolase (FBA) carrying six His on the C-end was purified by affinity metal chelating chromatography. The Mc.
O N, Rozova +4 more
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[36] Fructose-1,6-bisphosphate aldolase from Bacillus subtilis
1982Publisher Summary This chapter describes an assay to determine the aldolase activity by coupled spectrophotometric (methods A–C) and colorimetric assay. In assay method A, aldolase activity can be determined by measuring the rate of glyceraldehyde 3-phosphate formation by aldolase from fructose 1,6-bisphosphate.
Susumu Ujita, Kinuko Kimura
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New highly selective inhibitors of class II fructose-1,6-bisphosphate aldolases
Bioorganic & Medicinal Chemistry Letters, 2004Phosphoglycolo amidoxime and phosphoglycolo hydrazide, two new derivatives of phosphoglycolic acid, were synthesised and successfully tested as selective competitive inhibitors of class II FBP-aldolases.
Matthieu, Fonvielle +3 more
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Cloning and Characterization of Schistosoma mansoni Fructose-1,6-Bisphosphate Aldolase Isoenzyme
The Journal of Parasitology, 1998A Schistosoma mansoni cercarial cDNA expression library, constructed in lambda gt11, was screened using the IgG fraction of sera taken from rabbits vaccinated with irradiated cercariae. A positive cDNA clone (1,431 base pairs) was selected and characterized.
E, El-Dabaa +7 more
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Rapid purification of fructose-1,6-bisphosphate aldolase from spinach chloroplasts
Photosynthesis Research, 1988A rapid procedure for the purification of fructose-1,6-bisphosphate aldolase from spinach chloroplasts is presented which involves two steps; precipitation of bulk protein with polyethylene glycol and partitioning of remaining soluble protein in aqueous two-phase systems. A 94% pure preparation is obtained within 6h with a yield of 19%.
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Initiating a crystallographic study of a class II fructose-1,6-bisphosphate aldolase
Journal of Molecular Biology, 1992We have reproducibly crystallized the metal-dependent Class II fructose-1,6-bisphosphate aldolase from Escherichia coli. Crystals in the shape of truncated hexagonal bipyramids have unit cell dimensions of a = b = 78.4 A, c = 290.6 A and are suitable for a detailed structural analysis.
J H, Naismith +9 more
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Microbiology, 2013
The thermotolerant Gram-positive methylotroph Bacillus methanolicus is able to grow with methanol, glucose or mannitol as a sole carbon and energy source. Fructose 1,6-bisphosphate aldolase (FBA), a key enzyme of glycolysis and gluconeogenesis, is encoded in the genome of B.
Stolzenberger, Jessica +2 more
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The thermotolerant Gram-positive methylotroph Bacillus methanolicus is able to grow with methanol, glucose or mannitol as a sole carbon and energy source. Fructose 1,6-bisphosphate aldolase (FBA), a key enzyme of glycolysis and gluconeogenesis, is encoded in the genome of B.
Stolzenberger, Jessica +2 more
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Characterization of a Mn-dependent Fructose-1,6-bisphosphate Aldolase in Deinococcus radiodurans
Biometals, 2006The key enzyme of the glycolytic pathway of Deinococcus radiodurans, fructose-1,6-bisphosphate aldolase, could be induced independently by glucose and Mn. The enzyme exhibited the characteristics of the metal-dependent Class II aldolases. Unlike most Class II aldolases, the deinococcal aldolase preferred Mn, not Zn, as a cofactor.
Yong-Mei, Zhang +3 more
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