Results 291 to 300 of about 324,763 (345)
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Molecular Characterization of Escherichia coli Malate Synthase G
European Journal of Biochemistry, 1994Two genes encoding the enzymes malate synthase G and glycolate oxidase, have been linked to locus glc (64.5 min), responsible for glycolate utilization in Escherichia coli. The gene encoding malate synthase G, for which we propose the notation glcB, has been cloned, sequenced and found to correspond to a 2262‐nucleotide open‐reading frame, which can ...
I, Molina +4 more
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European Journal of Biochemistry, 1991
A cDNA clone encoding the glyoxysomal malate synthase (EC 4.1.3.2) was identified by immunoscreening of a cDNA expression library constructed from poly(A)‐rich RNA of etiolated pumpkin cotyledons. Determination of the DNA sequence of the 1979‐nucleotide cDNA revealed a 1698‐nucleotide open reading frame that encodes a polypeptide of 64632 Da.
H, Mori +3 more
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A cDNA clone encoding the glyoxysomal malate synthase (EC 4.1.3.2) was identified by immunoscreening of a cDNA expression library constructed from poly(A)‐rich RNA of etiolated pumpkin cotyledons. Determination of the DNA sequence of the 1979‐nucleotide cDNA revealed a 1698‐nucleotide open reading frame that encodes a polypeptide of 64632 Da.
H, Mori +3 more
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Determination of malate synthase activity in polyacrylamide gels
Analytical Biochemistry, 1974Abstract It is shown that the generation of the insoluble precipitate, copper ferrocyanide, provides a distinct, rapid, and sensitive method for localizing malate synthase in polyacrylamide gels. Both enzymes of the glyoxylate cycle, isocitrate lyase and malate synthase, can now be specifically stained using the same polyacrylamide gel system.
M J, Volk, R N, Trelease, H C, Reeves
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Malate synthase: Aggregation, deaggregation, and binding of phospholipids
Archives of Biochemistry and Biophysics, 1983Octameric malate synthase is located in the glyoxysomes of cucumber cotyledons. The enzyme is predominantly confined to the organelle's membrane and can be solubilized with Mg2+. Separation of cell structures in a zonal rotor afforded, besides glyoxysomes, two other zones with malate synthase activity, viz., in the gradient supernatant and in the range
C, Kruse, H, Kindl
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A functionally active dimer of Mycobacterium tuberculosis Malate synthase G
European Biophysics Journal, 2010Malate synthase G is an important housekeeping enzyme of glyoxylate shunt in mycobacterium. The pleotropic function of this protein by virtue of its intracellular/extracellular localization and its behavior as an adhesin and virulence factor is quite enigmatic.
Ranjeet Kumar, V. Bhakuni
semanticscholar +3 more sources
Particulate isocitrate lyase and malate synthase in Caenorhabditis elegans
Archives of Biochemistry and Biophysics, 1977Abstract Biochemical evidence is presented suggesting the particulate nature of some of the glyoxylate cycle enzymes in the free-living nematode Caenorhabditis elegans . A crude homogenate of freshly grown nematodes was prepared by gentle grinding.
T R, Patel, B A, McFadden
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Mycobacterium tuberculosis malate synthase is a laminin‐binding adhesin
Molecular Microbiology, 2006Summary Mycobacterium tuberculosis (M. tb) uses the glyoxalate bypass for intracellular survival in vivo. These studies provide evidence that the M. tb malate synthase (MS) has adapted to function as an adhesin which binds to laminin and fibronectin. This binding is achieved via the unique C‐terminal region of the M. tb MS.
A. Kinhikar +6 more
semanticscholar +3 more sources
Post-irradiation inactivation of the sulfhydryl enzyme malate synthase
Biochemical and Biophysical Research Communications, 1984The sulfhydryl enzyme malate synthase was inactivated in air-saturated aqueous solution by X-irradiation (2 kGy). Changes of activity were registered up to 60 h after irradiation. Effects of specific additives (formate, superoxide dismutase, catalase), added before and/or after irradiation, revealed the role of the deleterious radical and non-radical ...
H, Durchschlag, P, Zipper
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Citrate synthase and malate dehydrogenase from tomato fruit
Phytochemistry, 1988Abstract The purification of citrate synthase and malate dehydrogenase from tomato fruit is described. Citrate synthase has a total M r of approximately 104 000 and a subunit M r of approximately 50 000, indicating a dimer of similar sized subunits. K m values for oxaloacetate and acetyl-CoA are 19 and 18 μM respectively.
D. Jeffery +2 more
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Hydrogen peroxide induced oxidation of peroxisomal malate synthase and catalase
Archives of Biochemistry and Biophysics, 2009Peroxisomes contain oxidases that produce H(2)O(2), which can result in protein oxidation. To test the vulnerability of peroxisomal proteins to oxidation in vivo the organelles were isolated from castor bean endosperm incubated with H(2)O(2).
Pria, Anand +3 more
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