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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, Petr Zuman
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Inhibition of phenol sulfotransferase by pyridoxal phosphate

Biochemical Pharmacology, 1994
The biologically abundant cofactor, pyridoxal-5-phosphate (PLP), is a potent inhibitor of bovine phenol (aryl) sulfotransferase (PST). Preincubation of purified enzyme with as little as 1 microM PLP decreased PST activity by 50%. Excess 2-naphthol protected PST from inactivation by PLP, whereas 2-naphthyl sulfate and PAPS were not protective.
Joe D. Beckmann, Ron Bartzatt
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Activation of DOPA decarboxylase by pyridoxal phosphate

Archives of Biochemistry and Biophysics, 1962
Abstract DOPA decarboxylase from rat liver was purified by chromatography on DEAE-Sephadex. The purified enzyme decarboxylates o-tryosine, m-tyrosine, DOPA and 5-hydroxytryptophan at different rates. The pH optimum for all substrates was found to be 7.2. The enzyme has the characteristic absorption spectrum of other pyridoxal enzymes, thus indicating
Jorge Awapara   +2 more
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Pyridoxal Phosphate: a Coenzyme for Histidine Decarboxylase

Nature, 1959
ALTHOUGH the role of pyridoxal phosphate as a coenzyme of amino-acid decarboxylases is generally recognized, attempts to demonstrate its participation in the enzymic decarboxylation of histidine have hitherto been unsuccessful ...
S. Ono, P. Hagen
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Fluorometric determination of pyridoxal phosphate in enzymes

Analytical Biochemistry, 1969
Abstract The pyridoxal phosphate contents of several enzymes have been compared both by fluorometry and by absorption spectrophotometry of the phenylhydrazone, and give results in good agreement. The fluorometric method is as rapid and simple as the spectrophotometric method and in addition is about as sensitive as the best biological assay methods ...
openaire   +5 more sources

Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.

Annual Review of Biochemistry, 2003
Pyridoxal phosphate (PLP)-dependent enzymes are unrivaled in the diversity of reactions that they catalyze. New structural data have paved the way for targeted mutagenesis and mechanistic studies and have provided a framework for interpretation of those ...
A. C. Eliot, J. Kirsch
semanticscholar   +1 more source

Inactivation of Rhodanese by Pyridoxal 5′‐Phosphate

European Journal of Biochemistry, 1975
Pyridoxal 5′‐phosphate and other aromatic aldehydes inactivate rhodanese. This inactivation reaches higher extents if the enzyme is in the sulfur‐free form. The identification of the reactive residue as an amino group has been made by spectrophotometric determination of the 5′‐phosphorylated pyridoxyl derivative of the enzyme.
Doriano Cavallini   +4 more
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Pyridoxal phosphate and hypertensive disorders of pregnancy

American Journal of Obstetrics and Gynecology, 1975
Pyridoxal phosphate (vitamin B6) concentrations in peripheral and cord blood obtained at the time of delivery were measured in 30 women. The average plasma concentration in nine women with normal pregnancy was 4.3 ng. per milliliter; in 10 women with pre-eclampsia, 3.3 ng. per milliliter; and in nonpregnant women, 17 ng. per milliliter.
Michael Haas Brophy, Pentti K. Siiteri
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Plasma pyridoxal phosphate in diabetics

The American Journal of Clinical Nutrition, 1984
A Hamfelt, L Soderhjelm
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