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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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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.
T, Hirakawa-Sakurai +2 more
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Inactivation of microbial pyridoxal kinase by pyridoxal.
Acta vitaminologica et enzymologica, 1982Pyridoxal kinase from Escherichia coli and bakers' yeast was inactivated by pyridoxal while the enzyme from rat and pig brain was not. The inactivation of the enzyme purified from E. coli was reversible and was rendered irreversible by the reduction with NaBH4.
Y, Furukawa, R, Yamada, A, Iwashima
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INTERRELATIONSHIPS BETWEEN PYRIDOXAL PHOSPHATE AND PYRIDOXAL KINASE IN RABBIT BRAIN1
Journal of Neurochemistry, 1970Abstract—An inverse relationship was demonstrable between the concentration of pyridoxal phosphate and the activity of pyridoxal kinase in rabbit brain. The administration of pyridoxine elevated the concentration of pyridoxal phosphate and decreased the activity of pyridoxal kinase.
M. S. Ebadi, E. E. McCoy, R. B. Kugel
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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.
J A, Kerry, F, Kwok
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Bombyx mori Pyridoxal Kinase cDNA Cloning and Enzymatic Characterization
Journal of Genetics and Genomics, 2007Pyridoxal kinase (PLK) (EC 2.7.1.35) catalyzes the ATP-dependent phosphorylation of pyridoxal, generating pyridoxal-5.-phosphate (PLP), an important cofactor for many enzymatic reactions. Bombyx mori, similar to mammals, relies on a nutritional source of vitamin B6 to synthesize PLP. This article describes how a cDNA encoding PLK was cloned from Bombyx
Ruijun, Shi +3 more
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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.
P, Dominici, F, Kwok, J E, Churchich
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Structure-Function Relationships of Porcine Pyridoxal Kinase
2000Pyridoxal kinase (PK) catalyzes the formation of pyridoxal-5-phosphate (PLP) from pyridoxal (PL), ATP and a divalent cation (Zn2+). So far, there is no three-dimensional structure of PK available. Site-directed mutagenesis was carried out to study the importance of three conserved residues: Tyr137, Gly242 and G1y244. The mutants (Y137F, G242A and G244A)
Y. C. Leung +4 more
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