Prostatic acid phosphatase assay with self-indicating substrate 2,6-dichloro-4-acetylphenyl phosphate

1995 ◽  
Vol 41 (2) ◽  
pp. 200-203 ◽  
Author(s):  
S Osawa ◽  
S Iida ◽  
H Yonemitsu ◽  
K Kuroiwa ◽  
K Katayama ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Dynamic Range ◽  
Kinetic Method ◽  
High Specificity ◽  
Prostatic Acid Phosphatase ◽  
Molar Absorptivity ◽  
Total Acid ◽  
Phosphatase Assay

Abstract We characterized six self-indicating substrates, synthesized as the derivative compounds of acetylphenyl phosphate, for serum prostatic acid phosphatase (PAP) activity. One of the substrates, 2,6-dichloro-4-acetylphenyl phosphate (DCAPP), is superior to others in terms of stability, affinity, and low Km for PAP. The hydrolyzed product, 2,6-dichloro-4-acetylphenol (DCAP), has a maximum absorption at 334.2 nm, a pKa of 4.15, and a molar absorptivity at 340 nm of 21,490 L.mol-1.cm-1 in citrate-HCl buffer, pH 5.4. PAP activity was assessed by subtracting tartaric acid-inhibited acid phosphatase activity from total acid phosphatase activity. Our assay system involving DCAPP is a unique kinetic method that shows good reproducibility, wide analytical dynamic range, and high specificity for PAP. Moreover, it is easily adaptable to automated analyzers because the product, DCAP, can be monitored at 340 nm.

Kinetic Method for Determining Acid Phosphatase Activity in Serum with Use of the "CentrifiChem"

1972 ◽  
Vol 18 (8) ◽  
pp. 841-844 ◽  
Author(s):  
Diane L Fabiny-Byrd ◽  
Gerhard Ertingshausen
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Kinetic Method ◽  
Reaction Rates ◽  
Phosphatase Activities ◽  
Fast Red ◽  
Presence And Absence

Abstract Acid phosphatase activity is determined by splitting 1-naphthyl phosphate, concurrently diazotizing the released 1-naphthol with Fast Red TR, and measuring the resulting color. The test is performed in the presence and absence of tartrate. Reaction rates can be continuously monitored, and their difference is proportional to acid phosphatase activity that is inhibited by tartrate. Results for sera with normal and increased acid phosphatase activities are presented and three different methods for acid phosphatase are compared. The kinetic blank used in the reaction eliminates all nonenzymatic contributions to substrate splitting.

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

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.

Prostatic Acid Phosphatase Activity in the Postcoital Vagina

1975 ◽  
Vol 20 (4) ◽  
pp. 10313J ◽  
Author(s):  
K. L. McCloskey ◽  
G. C. Muscillo ◽  
B. Noordewier
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Prostatic Acid Phosphatase

ACID PHOSPHATASE ACTIVITY IN VIABLE AND REGRESSING RAT CORPORA LUTEA

1970 ◽  
Vol 47 (2) ◽  
pp. 167-176 ◽  
Author(s):  
JEANNE A. SMITH ◽  
H. B. WAYNFORTH
Keyword(s):  
Acid Phosphatase ◽  
Corpus Luteum ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Enzymic Activity ◽  
Corpora Lutea ◽  
Cellular Composition ◽  
Total Acid ◽  
Progesterone Secretion ◽  
Experimentally Induced

SUMMARY Free and total acid phosphatase activity has been measured in individual corpora lutea from rat ovaries in various reproductive states (both natural and experimentally induced). Significant changes both in weight and enzymic activity were found, and an attempt has been made to correlate these with the growth and regression of the corpora lutea. A possible connexion between acid phosphatase activity, progesterone secretion and/or cellular composition of the corpus luteum is suggested.

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