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Fluorimetric determination of beryllium with pyridoxal-5-phosphate
Talanta, 1985A simple, rapid and selective method for the determination of beryllium with pyridoxal-5-phosphate has been developed. The system is only fluorescent (lambda(ex) 360, lambda(em) 460 nm) in the presence of a nitrogenous base such as ammonia, ethylenediamine or pyridine, owing to the possible formation of a ternary complex.
A, Petidier +3 more
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Interaction of pyridoxal 5′ phosphate and malate dehydrogenase
Biochemical and Biophysical Research Communications, 1971Abstract Mitochondrial malate dehydrogenase (L-malate-NAD + oxidoreductase, E.C.1.1.1.37) of porcine heart is totally and irreversibly inhibited by pyridoxal-5′-phosphate. The course of inactivation appears to be biphasic in nature. The coenzyme, NADH, was observed to fully protect the enzyme from inactivation, suggesting interaction at or near the ...
F J, Yost, J H, Harrison
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Pyridoxal 5-Phosphate and Calcium Channels
2000The BAY K 8644 -induced influx of 45Calcium into intracellular compartment of artery segments of normal rats was blocked by pyridoxal phosphate (PLP) as well as by the dihydropyridine-sensitive calcium channel antagonists (CCA). PLP also decreased bindingin vitroof CCA to membrane preparations from normal vascular tissue.
Krishnamurti Dakshinamurti +4 more
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Pyridoxal 5 phosphate for neuroleptic-induced tardive dyskinesia
Cochrane Database of Systematic Reviews, 2013Tardive dyskinesia is a chronic and disabling abnormal movement disorder affecting the muscles of the face, neck, tongue and the limbs. It is a common side effect of long-term antipsychotic medication use in individuals with schizophrenia and other related psychotic disorders. While there are no known effective treatments for tardive dyskinesia to date,
Adegoke Oloruntoba, Adelufosi +2 more
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Acetylcholinesterase is not inhibited by pyridoxal 5′-phosphate
Biochimica et Biophysica Acta (BBA) - General Subjects, 1986Acetylcholinesterase activity was assayed in the absence and presence of pyridoxal 5'-phosphate. If substrate hydrolysis was measured by the pH-stat method, its rate was not significantly affected by pyridoxal 5'-phosphate. In the spectrophotometric assay, however, this compound led to an apparent decrease in rate.
R, Gentinetta, U, Brodbeck
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Pyridoxal–5′–Phosphate and Alkaline Phosphatase
Hepatology, 1986Markedly increased circulating concentrations of pyridoxal–5′–phosphate (PLP) were found in each of 14 patients representing all clinical forms of hypophosphatasia, an inborn error characterized by deficient activity of the tissue–nonspecific (bone/liver/kidney) isoenzyme of alkaline phosphatase (AP).
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Pyridoxal 5′-phosphate assay based on lucigenin chemiluminescence
Microchimica Acta, 2018The authors describe the first chemiluminescence (CL) based method for determination of pyridoxal 5'-phosphate (PLP). PLP is found to generate intense CL with lucigenin higher than that of the conventional lucigenin-H2O2 system by a factor of about 9.0.
Mohamed Ibrahim Halawa +5 more
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P2 purinoceptor antagonist properties of pyridoxal-5-phosphate
European Journal of Pharmacology, 1994The antagonist properties of pyridoxal-5-phosphate, a synthesis precursor of pyridoxalphosphate-6-azophenyl-2',4'-disulphonic acid, were investigated on P2 purinoceptor-mediated responses of the rat isolated vagus nerve and vas deferens. In addition, the effect of this agent was studied on high affinity tritiated alpha,beta-methylene adenosine ...
Derek J. Trezise +5 more
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Design of Pyridoxal 5"-Phosphate Dependent Catalytic Antibodies
Biochemistry (Moscow), 2002Modern approaches for developing antibodies with coenzyme-dependent activities are discussed for pyridoxal 5'-phosphate dependent transformation of amino acid as an example. A new type of antigens analogous to enzyme--substrate compounds is suggested for the production of such antibodies.
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Regulation of pyridoxal 5′-phosphate metabolism in liver
Biochemical and Biophysical Research Communications, 1974Abstract The pyridoxal 5′-phosphate content of liver in vivo and of hepatocytes in vitro remains unaltered in the presence of excess unphosphorylated vitamin B6 precursors. Studies with isolated hepatocytes and subcellular fractions show that while product inhibition of pyridoxine phosphate oxidase does not limit synthesis sufficiently to
T K, Li, L, Lumeng, R L, Veitch
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