hymecromone has been researched along with phenylphosphonic-acid* in 1 studies
1 other study(ies) available for hymecromone and phenylphosphonic-acid
Article | Year |
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Specific detection and properties of enzyme hydrolyzing phosphonate ester in serum.
An enzyme capable of hydrolyzing 4-methylumbelliferyl phenylphosphonate to 4-methylumbelliferone and phenylphosphonic acid has been detected in human serum. It has a Km value of 1.72 x 10(-4) mol/L, has an optimum pH of 8.8-9.1 in Tris buffer, and shows maximum activity at 60 degrees C (30 min). The enzymic activity can be inhibited by Na3PO4, EDTA, and cysteine. We saw no effect of CuSO4, adenosine, thymidine, NaN3, diethyl p-nitrophenyl phosphate, p-chloromercuribenzoate, isopropyl fluorophosphate, or eserine on the enzymic activity. The enzyme cannot hydrolyze substrates of phosphodiesterase I or alkaline phosphatase. The enzyme is considered a phosphonate esterase. Topics: Adolescent; Child; Child, Preschool; Enzyme Stability; Esterases; Female; Humans; Hydrogen-Ion Concentration; Hymecromone; Infant; Kinetics; Organophosphonates; Organophosphorus Compounds; Pregnancy; Reference Values; Substrate Specificity; Temperature | 1992 |