Kinetics of Hydrolysis of p-Nitrophenyl Phosphate by Fowl Plasma Alkaline Phosphatase
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چکیده
منابع مشابه
A menadione-dependent enzymatic hydrolysis of p-nitrophenyl phosphate.
Sonic extracts of Clostridium sticklandii contain an enzyme that hydrolyzes p-nitrophenyl phosphate to yield equivalent amounts of p-nitrophenol and orthophosphate. A large number of common phosphate esters is not decomposed. The most striking property of the bacterial enzyme is its dependence on both menadione (2-methyl-1,4-napthoquinone or vitamin Ka) and sulfhydryl compounds for activity, Th...
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1. The steady-state rate of hydrolysis of 2,4-dinitrophenyl phosphate catalysed by Escherichia coli phosphatase is identical with that of 4-nitrophenyl phosphate over the pH range 5.5-8.5. 2. The increase in the rate of the enzyme-catalysed decomposition of nitrophenyl phosphates in the presence of tris at pH8.1 and 5.9 is consistent with the hypothesis that tris increases the rate of decomposi...
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The repressible alkaline phosphatase of Escherichia coli (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1) promises to play a role in biochemical genetics comparable to that played by fl-galactosidase (l-5). It is also being used increasingly for class experiments. The evaluation of the important characteristic kinetic constants for this enzyme, however, poses certain technical difficult...
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We studied 53 lots of 4-nitrophenyl phosphate (I), obtained from 20 different commercial suppliers, and used this information to set specifications for it. Using these well-defined specifications, we classified 21 lots of I as "unacceptable," 26 lots as "borderline," and six as "acceptable." All lots were shown to contain some 4-nitrophenol and inorganic phosphate. However, "acceptable" I had <...
متن کاملPresteady State Kinetics of Phosphoro - thioate Hydrolysis by Alkaline Phosphatase RATE - LIMITING DEPHOSPHORYLATION
The hydrolysis of 0-p-phenylazophenylphosphorothioate by Escherichia coli alkaline phosphatase was studied by the stopped-flow technique. “Burst” kinetics is observed at both acid and basic pH, suggesting that a step following thiophosphorylation is rate-limiting at all pH values. At pH 8.5, activation of a second active site on the enzyme dimer is observed in the transient phase as subsrrate c...
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ژورنال
عنوان ژورنال: Poultry Science
سال: 1969
ISSN: 0032-5791
DOI: 10.3382/ps.0481311