Results 51 to 60 of about 69 (69)
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Cloning and characterization of Arabidopsis thaliana pyridoxal kinase
Planta, 2002Pyridoxal kinase (PK; EC 2.7.1.35), a key enzyme in vitamin B(6) metabolism, was cloned from Arabidopsis thaliana (L.) Heynh. and characterized. The amino acid sequence of the A. thaliana PK was found to be similar to the mammalian enzyme, with a homology of more than 40%. Characterization studies showed that the kinase is a dimeric molecule consisting
Francis Kwok +2 more
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A rapid fluorometric assay for erythrocyte pyridoxal kinase
Biochemical Medicine, 1982Abstract We describe a method for measurement of erythrocyte pyridoxal kinase activity in hemolysates, in which pyridoxal phosphate is oxidized and assayed by fluorometry. We also use this method to measure pyridoxal phosphate synthesis by intact erythrocytes suspended with pyridoxal or pyridoxine.
M.J. Haut +4 more
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Purification and Properties of Pyridoxal Kinase from Bovine Brain
Molecular and Cellular Biochemistry, 1993A 27,000-fold purification of pyridoxal kinase from bovine brain tissue has been achieved by a combination of ammonium sulfate fractionation, DEAE-cellulose chromatography, hydroxyapatite chromatography, Sephadex G-150 gel filtration, Blue Sepharose CL-6B chromatography, and Phenyl-Superose chromatography.
Makoto Matsuda +2 more
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Pyridoxal kinase activity in blood cells
Clinica Chimica Acta, 1967Abstract The activity of the pyridoxal phosphate-forming enzyme, pyridoxal kinase, has been demonstrated in erythrocytes and leucocytes. The activity in erythrocytes was found to be 197 ± 18 · 10 −9 (M ± S.E.M) ng pyridoxal phosphate/h/cell (1.33 ± 0.12 · 10 −11 nmoles/min/cell) and in leucocytes between 29.7 ± 7.9 · 10 −6 (M ± S.E.M.) ng ...
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Enzyme and Microbial Technology, 2017
Cadaverine, a five-carbon diamine (1,5-diaminopentane), can be made by fermentation or direct bioconversion and plays an important role as a building block of polyamides. Lysine decarboxylase (CadA) transforms L-lysine to cadaverine and pyridoxal 5'-phosphate (PLP) can increases conversion rate and yield as a cofactor.
Jun-Young Kim +9 more
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Cadaverine, a five-carbon diamine (1,5-diaminopentane), can be made by fermentation or direct bioconversion and plays an important role as a building block of polyamides. Lysine decarboxylase (CadA) transforms L-lysine to cadaverine and pyridoxal 5'-phosphate (PLP) can increases conversion rate and yield as a cofactor.
Jun-Young Kim +9 more
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Pyridoxal kinase in the human placenta and foetus through gestation
Clinica Chimica Acta, 1969Abstract The presence of the pyridoxal phosphate forming enzyme, pyridoxal kinase, has been demonstrated in the human placenta and foetal liver and kidney, and properties of the placental enzyme have been investigated. K m value for pyridoxal was found to be 3.3 × 10 −4 M for the placental kinase.
B. Shane, S.F. Contractor
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Activity of Pyridoxamine as a Substrate for Brain Pyridoxal Kinase
Journal of Neurochemistry, 1980AbstractThe substrate activity of pyridoxamine (PM) for brain pyridoxal (PL) kinase was examined in view of a recent report which indicated that PM was a poor substrate for this enzyme. Bovine brain PL kinase was shown by liquid chromatography to catalyze the phosphorylation of PM (Km= 65 μm).
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Purification and Characterization of Pyridoxal Kinase from Human Erythrocytes
Preparative Biochemistry, 1986Pyridoxal kinase has been purified 50,000-fold from human erythrocytes. The purification procedure included dextran-induced aggregation of red blood cells, ammonium sulphate fractionation of the haemolysate, DEAE-cellulose chromatography, hydroxyapatite chromatography. Sephadex G-100 gel filtration and omega-aminooctyl agarose chromatography.
F Kwok, J A Kerry
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Effects of tetrahydroisoquinolines on dopa decarboxylase and pyridoxal kinase
Drug Development Research, 1981AbstractThe mechanism of the nullification of the therapeutic effects of levodopa by pyridoxine in parkinsonian patients is not known and is still a subject of much speculation. Among other suggestions, it has been proposed that pyridoxine and levodopa may form tetrahydroisoquinoline derivatives in vivo, which may in turn inhibit dopa decarboxylase or ...
Piyarat Govitrapong, Manuchair Ebadi
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Proteolytic cleavage of pyridoxal kinase into two structural domains
Biochimie, 1989Chymotryptic digestion of sheep brain pyridoxal kinase, a dimer of identical subunits each of 40 kDa, yields 2 fragments of 24 and 16 kDa with concomitant loss of catalytic activity. These fragments were separated by chromatographic techniques and analyzed for interaction with the ATP analogue, trinitrophenyl-ATP, using fluorescence spectroscopy.
Paola Dominici +2 more
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