Automated Determination of Serum Alkaline Phosphatase Using a Modified Bodansky Technic

1964 ◽  
Vol 10 (1) ◽  
pp. 75-82 ◽  
Author(s):  
H Keay ◽  
J A Trew
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Inorganic Phosphate ◽  
Serum Alkaline Phosphatase ◽  
Automated Determination

Abstract An automated procedure for the measurement of alkaline phosphatase activity by a modification of the Bodansky method is described. It has been possible to adapt the Fiske-SubbaRow method for phosphate so that alkaline phosphatase is determined by a second run, immediately following the determination of inorganic phosphate. Studies of the effect of time, pH, and concentration of barbital on the enzyme activity are discussed, and the advantages of the method are listed.

Use of N-methyl-D-glucamine as buffer in the determination of serum alkaline phosphatase activity.

1981 ◽  
Vol 27 (10) ◽  
pp. 1729-1732 ◽  
Author(s):  
V Chromý ◽  
L Zahradnícek ◽  
J Voznícek
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Serum Alkaline Phosphatase ◽  
Reaction Conditions ◽  
Serum Alkaline Phosphatase Activity ◽  
Nitrophenyl Phosphate ◽  
Optimum Reaction ◽  
Assay Conditions

Abstract We describe a method for determining serum alkaline phosphatase activity with use of N-methyl-D-glucamine buffer, Na+ is a definite activator, whereas NH4+ and Li+ inhibit enzyme activity. Optimum reaction conditions are: methylglucamine buffer, 0.35 mol/L, pH 10.2 +/- 0.1 (30 degrees C); NaCl, 70 mmol/L; MgCl2, 0.5 mmol/L; disodium 4-nitrophenyl phosphate, 15 mmol/L; reaction temperature, 30 degrees C; reaction time, 2 min. The assay conditions are optimum for all human serum isoenzymes.

Study of Optimum Buffer Conditions for Measuring Alkaline Phosphatase Activity in Human Serum

1972 ◽  
Vol 18 (2) ◽  
pp. 97-104 ◽  
Author(s):  
Robert B McComb ◽  
George N Bowers
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Human Serum ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Serum Alkaline Phosphatase ◽  
Buffer Concentration ◽  
Optimal Conditions ◽  
Serum Alkaline Phosphatase Activity ◽  
Ph Buffer

Abstract We have compared 23 compounds, with and without transphosphorylating properties, as buffer systems for human serum alkaline phosphatase activity, with p-nitrophenylphosphate as substrate. Relative enzyme activity in four representative buffers at near-optimal conditions was ethylaminoethanol > diethanolamine > 2-amino-2-methyl-1-propanol > carbonate. Transphosphorylation was demonstrated in the two buffers in which the enzyme was most active, ethylaminoethanol and diethanolamine. The optima for pH, buffer concentration, and substrate for these four systems were studied in detail. 2-Ethylaminoethanol supports the highest enzyme activity of any of the compounds tested. Diethanolamine was shown to have many of the favorable characteristics required for a reference enzyme procedure.

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