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Reaction of dithionite and bisulfite with pyridoxal and pyridoxal enzymes

Analytical Biochemistry, 1969
Abstract Both bisulfite and dithionite produce marked changes in the spectra of pyridoxal, pyridoxal phosphate, and pyridoxal phosphate enzymes. The spectrum of pyridoxal phosphate in bisulfite solutions resembles that of the addition product of pyridoxal phosphate with cysteine.
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Transport and Metabolism of Pyridoxal and Pyridoxal Phosphate in the Small Intestine of the Rat

The Journal of Nutrition, 1979
The vascularly perfused small intestine of the rat was utilized to study the absorption and metabolism of pyridoxamine (PM) and pyridoxamine-5'-phosphate (PMP), independent of other tissues including erythrocytes. [3H]PM or [3H]PMP was administered intralumenally with or without the addition of unlabeled PM, or PMP or inorganic phosphate.
H, Mehansho, M W, Hamm, L M, Henderson
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Neuroprotective Effects of Pyridoxal Phosphate and Pyridoxal against Ischemia in Monkeys

Nutritional Neuroscience, 2001
Previously, in monkeys undergoing 20 min whole brain ischemia we demonstrated that the activated calpain-induced lysosomal disruption with the resultant leakage of cathepsins B and L, causes neuronal death in the cornu Ammonis (CA) 1 sector on day 5.
T, Yamashima   +4 more
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Pyridoxal Derivatives in Transamination

Nature, 1952
IN living systems a transfer of amino groups occurs between certain amino-acids and keto-acids. This important reversible process, known as ‘transamination’1, effects a link between carbohydrate and protein metabolism, and the responsible enzymes, the transaminases, are activated by pyridoxal2 or pyridoxamine phosphates3. The proposed mechanisms of the
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Direct polarographic determination of pyridoxal in the presence of pyridoxal-5-phosphate

Collection of Czechoslovak Chemical Communications, 1962
The determination of pyridoxal in the presence of pyridoxal-5-phosphate may be1 based on the difference between the total wave-height obtained at pH about 9, where both substances give a diffusion-controlled wave and that obtained in acid media, where pyridoxal alone shows a kinetic current2.
O. Manoušek, P. Zuman
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Luminescence spectroscopy of pyridoxic acid and pyridoxic acid bound to proteins

European Journal of Biochemistry, 1994
Luminescence techniques, i.e. fluorescence and phosphorescence, have been employed to study pyridoxic acid bound to proteins through a stable amide linkage. Proteins tagged with 4‐pyridoxic acid display the following fluorescence properties: (a) emission and excitation spectra centered at around 430 and 320 nm, respectively; (b) fluorescence quantum ...
O S, Kwon, M, Blazquez, J E, Churchich
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Pyridoxal-specific antibodies obtained with a synthetic pyridoxal-polypeptide conjugate

Biochimica et Biophysica Acta (BBA) - General Subjects, 1966
Abstract The attachment of pyridoxal to a non-antigenic synthetic branched polypeptide resulted in an immunogenic macromolecule, capable of eliciting in rabbits antibodies with specificity directed against the pyridoxal moiety. The anti-pyridoxal antibodies were purified immunospecifically, making use of ion-exchange chromatography in 8 M urea.
H, Ungar-Waron, M, Sela
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Assay of pyridoxal-5'-phosphate, pyridoxal and pyridoxic acid in biological material.

International journal for vitamin and nutrition research. Internationale Zeitschrift fur Vitamin- und Ernahrungsforschung. Journal international de vitaminologie et de nutrition, 1990
The two vitamin B6-vitamers having an aldehyde function are oxidised to the corresponding acids and subjected to an HPLC separation on an RP 18 phase with a solvent consisting of 5% methanol in phosphate buffer at pH 3.5. The detection is carried out by fluorometry with excitation at 318 nm and emission at 418 nm.
D, Hess, J P, Vuilleumier
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Inactivation of microbial pyridoxal kinase by pyridoxal.

Acta vitaminologica et enzymologica, 1982
Pyridoxal 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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Modification of intracellular hemoglobin with pyridoxal and pyridoxal 5'-phosphate.

Blood cells, 1983
The aldehyde forms of vitamin B6, pyridoxal and pyridoxal 5'-phosphate (PLP) have aroused interest as antisickling agents because of their ability to modify hemoglobin (Hb) and their low toxicity. To study their rate of formation and stability inside red cells, pyridoxal-Hb and PLP-Hb were measured in lysates from treated normal and sickle erythrocytes
J A, Kark   +5 more
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