Abstract
AbstractThe present paper reports on the study of the dephosphorylation of pyridoxal 5′‐phosphate and four derived hydrazones (containing the residues of pyrazine, 2‐furan, 2‐thiophene, 3‐pyridine carboxylic acids) induced by bovine alkaline phosphatase from intestinal mucosa at 298.2 K and pH 10 (0.05 m Tris–HCl buffer). We observed and discussed characteristic changes in the UV–vis and fluorescent spectra of substrates. Michaelis–Menten parameters of the enzymatic dephosphorylation are calculated. The stability of alkaline phosphatase in the presence of hydrazones is confirmed. The dephosphorylation of the Zn(II) complex with pyridoxal 5′‐phosphate‐derived hydrazone is analyzed.
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