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.

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.

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.

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

Spectrophotometric and liquid-chromatographic studies of thymolphthalein monophosphate. Specifications for high-quality substrate for the measurement of prostatic acid phosphatase activity.

1981 ◽  
Vol 27 (8) ◽  
pp. 1372-1377 ◽  
Author(s):  
G N Bowers ◽  
M Onoroski ◽  
R S Schifreen ◽  
L R Brown ◽  
R E Klem ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Prostatic Acid Phosphatase ◽  
Enzymic Activity ◽  
Disodium Salt ◽  
Critical Importance ◽  
High Quality ◽  
Activity Measurements ◽  
Liquid Chromatographic

Abstract Fourteen lots of thymolphthalein monophosphate (TMP), disodium salt, obtained from 10 commercial suppliers were compared spectrophotometrically at 445 and 595 nm, liquid-chromatographically with monitoring at 254 nm, and enzymically by measurements of activity of prostatic acid phosphatase in human serum. Eight lots were classified as "unacceptable," six as "acceptable." Spectrophotometric testing revealed four lots with excessive thymolphthalein and three lots with grossly deficient amounts of TMP. In general, the chromatographic results paralleled those obtained by spectrophotometry, and both results correlated well with enzymic activity. Changing water content in this hygroscopic salt was a major problem, which resulted in great uncertainty as to the formula weight and therefore as to the moles of TMP actually taken. From these studies, specifications for high-quality TMP were determined. The critical importance of simultaneous enzymic activity measurements in comparisons with other "acceptable" lots in defining an adequate TMP substrate is stressed. Use of these specifications for selecting TMP for acid phosphatase activity measurements should improve intra- and inter-laboratory analytical performance.

Prostatic acid phosphatase activity in carcinoid tumors

Cancer ◽  
1986 ◽  
Vol 58 (1) ◽  
pp. 136-138 ◽  
Author(s):  
Leslie H. Sobin ◽  
Brent M. Hjermstad ◽  
Isabell A. Sesterhenn ◽  
Elson B. Helwig
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Prostatic Acid Phosphatase ◽  
Carcinoid Tumors
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