Automated Determination of Acid Phosphatase

1966 ◽  
Vol 12 (4) ◽  
pp. 226-233 ◽  
Author(s):  
Bernard Klein ◽  
Morris Oklander ◽  
Stanley Morgenstern
Keyword(s):  
Acid Phosphatase ◽  
Human Serum ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Prostatic Acid Phosphatase ◽  
Biological Materials ◽  
Automated System ◽  
Automated Determination ◽  
Serum Acid Phosphatase

Abstract A procedure is presented for the automated determination of acid phosphatase activity in biological materials using the Robot Chemist. Although either phenylphosphate and α-naphthylphosphate may be used as substrate in this analysis, the procedure is described in detail for serum acid phosphatase using α-naphthylphosphate in 0.1 M citrate, pH 5.2, since this substrate is more selective for prostatic acid phosphatase in human serum. Enzymically generated aα- naphthol is determined by the Emerson reaction (alkaline aminoantipyrine and ferricyanide), modified for use with this automated system. Correlations are presented between the results obtained on the Robot Chemist and the identical procedure developed for the AutoAnalyzer.

Automated Determination of Acid Phosphatase

1965 ◽  
Vol 11 (11) ◽  
pp. 998-1008 ◽  
Author(s):  
Bernard Klein ◽  
Joseph Auerbach ◽  
Stanley Morgenstern
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Biological Materials ◽  
Flow Diagram ◽  
Animal Origin ◽  
Phenolic Substances ◽  
Automated Determination ◽  
Serum Acid Phosphatase

Abstract A procedure is presented for the automated determination of acid phosphatase activity in biological materials from either plant or animal origin. The Technicon N-7 flow diagram has been simplified, and the reagents for the measurement of enzymatically produced phenolic substances have been modified without loss of range or sensitivity. Both phenylphosphate and α-naphthylphosphate, introduced by Babson et al. (2, 3) for serum acid phosphatase, may be used as substrates. The Emerson reaction (alkaline aminoantipyrine and ferricyanide) with α-naphthol forms a more stable and reproducible color than the coupled product with tetrazotized o-dianisidine (Babson). Supporting data for these modifications are included.

Stabilization and Preservation of Serum Prostatic Acid Phosphatase Activity

1965 ◽  
Vol 11 (10) ◽  
pp. 943-950 ◽  
Author(s):  
Richard P Doe ◽  
George T Mellinger ◽  
Ulysses S Seal
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Prostatic Acid Phosphatase ◽  
Original Activity ◽  
Satisfactory Method ◽  
Effects Of Ph ◽  
The Stability ◽  
Serum Acid Phosphatase

Abstract The effects of pH and temperature of storage on the stability of the prostatic fraction of serum acid phosphatase activity have been studied in order to provide a satisfactory method for the preservation of activity in serums shipped from other hospitals. Addition of citrate tablets of a composition to buffer the serums at pH 6.2 was found to preserve the original activity at 25° for at least 7 days. These results were validated on a series of serums, subdivided into control and citrate-containing aliquots, shipped from the participating hospitals.

Improved determination of prostatic acid phosphatase (sodium thymolphthalein monophosphate substrate).

1976 ◽  
Vol 22 (5) ◽  
pp. 627-632 ◽  
Author(s):  
L M Ewen ◽  
R W Spitzer
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Enzyme Activities ◽  
Acid Phosphatase Activity ◽  
Prostatic Acid Phosphatase

Abstract We have modified a previously described method for determining acid phosphatase, with thymolphthalein monophosphate as substrate, to increase its sensitivity. We assessed effects of serum on variables influencing acid phosphatase activity as measured by this method. The method is shown to be not completely specific for prostatic acid phosphatase. The importance of standardizing methodology in measurement of enzyme activities is demonstrated.

An optimized continuous-monitoring procedure for semiautomated determination of serum acid phosphatase activity.

1976 ◽  
Vol 22 (12) ◽  
pp. 2025-2028 ◽  
Author(s):  
R Bais ◽  
J B Edwards
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Continuous Monitoring ◽  
Prostatic Acid Phosphatase ◽  
Monitoring Method ◽  
Modified Method ◽  
Nitrophenyl Phosphate ◽  
Monitoring Procedure

Abstract A continuous-monitoring method for measuring acid phosphatase activity with alpha-naphthyl phosphate as the substrate was critically evaluated and modified. Using partially purified prostatic acid phosphatase, we show that certain conditions for the assay must be satisfied to ensure linearity. These conditions include maintaining the pH between 5.6 and 5.9 and the addition of detergent to sustain linearity. The results obtained with alpha-naphthyl phosphate have been compared with those obtained by using p-nitrophenyl phosphate as substrate. When used with an automatic rate analyzer, the modified method is as sensitive but more reproducible.

Automated Determination of Acid Phosphatase

1966 ◽  
Vol 12 (5) ◽  
pp. 289-298 ◽  
Author(s):  
Bernard Klein ◽  
Joseph Auerbach
Keyword(s):  
Acid Phosphatase ◽  
Human Serum ◽  
Prostatic Acid Phosphatase ◽  
Inhibition Studies ◽  
Automated Determination

Abstract α-Naphthylphosphate is a selective substrate for the differentiation of prostatic acid phosphatase from erythrocytic acid phosphatase in human serum; its comparative specificity for prostatic enzyme is demonstrated by inhibition studies and by assay of mixtures of both enzymes in serum.

Determination of Acid Phosphatase Activity in Cells of Prostatic Tumours

Nature ◽  
1960 ◽  
Vol 188 (4751) ◽  
pp. 663-664 ◽  
Author(s):  
P. L. ESPOSTI ◽  
B. ESTBORN ◽  
J. ZAJICEK
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
In Cells
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