Prostatic Acid Phosphatase in Serum of Patients with Prostatic Cancer Is a Specific Phosphotyrosine Acid Phosphatase

Abstract We developed an assay to measure at acid pH the phosphotyrosine phosphatase activity in sera from patients with prostatic cancer. The method used quantifies the inorganic phosphate liberated from phosphotyrosine after incubation with serum, followed by the deproteinization of the reaction mixture. A high acid phosphatase (EC 3.1.3.2) activity towards phosphotyrosine was observed in all sera from patients with increased activity of prostatic acid phosphatase. This activity represented 96% of prostatic acid phosphatase and 77% of total acid phosphatase activities. Moreover, it was correlated (r = 0.91) with the amount of serum prostatic acid phosphatase determined by radioimmunoassay. When serum acid phosphatase activity was measured on several phosphorylated substrates, preferential hydrolysis was demonstrated for those in which the phosphate group was esterified on an aromatic ring rather than those presenting an aliphatic chain. Among phosphoamino acids, only phosphotyrosine was a good substrate, with little or no activity observed with phosphoserine and phosphothreonine. Human seminal plasma and partially purified prostatic acid phosphatase, tested for their activity on some of these substrates, gave similar results. On the other hand, sera from patients with above-normal alkaline phosphatase activity and no prostatic disease showed little or no activity on phosphotyrosine at both acid and alkaline pH values. Evidence is presented that the prostatic acid phosphatase in serum is a specific phosphotyrosine acid phosphatase.

Download Full-text

Unpredictable fluctuations in serum acid phosphatase activity in prostatic cancer

JAMA ◽

10.1001/jama.245.24.2501 ◽

1981 ◽

Vol 245 (24) ◽

pp. 2501-2504 ◽

Cited By ~ 7

Author(s):

W. D. Brenckman

Keyword(s):

Acid Phosphatase ◽

Phosphatase Activity ◽

Acid Phosphatase Activity ◽

Prostatic Cancer ◽

Serum Acid Phosphatase

Download Full-text

Acid phosphatase in Gaucher's disease.

Clinical Chemistry ◽

10.1093/clinchem/26.3.0371 ◽

1980 ◽

Vol 26 (3) ◽

pp. 371-382

Author(s):

D B Robinson ◽

R H Glew

Keyword(s):

Acid Phosphatase ◽

Phosphatase Activity ◽

Acid Phosphatase Activity ◽

Purification And Characterization ◽

Gaucher's Disease ◽

Gaucher’S Disease ◽

Intracellular Location ◽

Increased Activity ◽

Serum Acid Phosphatase

Abstract Increased acid phosphatase activity in the serum and tissues of patients with Gaucher's disease has now been recognized for two decades, but as yet no relation has been established between the enzyme and the etiology and progress of the disease. Here, we review results obtained by various investigators, ranging from a consideration of the methods used for the evaluation of serum acid phosphatase in Gaucher's disease to the most recent findings regarding the purification and characterization of two acid phosphatase isoenzymes from the spleen from patients with Gaucher's disease. We also discuss the intracellular location of tissue acid phosphatase in patients with Gaucher's disease and its contribution to the increased activity in serum.

Download Full-text

Automated Determination of Acid Phosphatase

Clinical Chemistry ◽

10.1093/clinchem/12.4.226 ◽

1966 ◽

Vol 12 (4) ◽

pp. 226-233 ◽

Cited By ~ 5

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.

Download Full-text

Unpredictable Fluctuations in Serum Acid Phosphatase Activity in Prostatic Cancer

JAMA ◽

10.1001/jama.1981.03310490019016 ◽

1981 ◽

Vol 245 (24) ◽

pp. 2501 ◽

Cited By ~ 20

Author(s):

Wayne D. Brenckman

Keyword(s):

Acid Phosphatase ◽

Phosphatase Activity ◽

Acid Phosphatase Activity ◽

Prostatic Cancer ◽

Serum Acid Phosphatase

Download Full-text

Counterimmunoelectrophoresis in determination of prostatic acid phosphatase in human serum.

Clinical Chemistry ◽

10.1093/clinchem/24.1.140 ◽

1978 ◽

Vol 24 (1) ◽

pp. 140-142 ◽

Cited By ~ 12

Author(s):

A G Foti ◽

J F Cooper ◽

H Herschman

Keyword(s):

Acid Phosphatase ◽

Human Serum ◽

Prostatic Cancer ◽

Serum Proteins ◽

Prostatic Acid Phosphatase ◽

Serum Samples ◽

Increased Activity ◽

Positive Results

Abstract We evaluated counterimmunoelectrophoresis for use in measuring prostatic acid phosphatase in detection of prostatic cancer. After staining for acid phosphatase, we could detect as little as 0.3 ng of purified enzyme standard complexed with antibody by this technique. However, when serum samples were used as antigen, the method was less sensitive (1.5-2.0 ng) because some of the serum proteins migrate with the phosphatase and decrease the intensity of the stain for acid phosphatase. For this reason we could not detect the phosphatase in serum samples of normal persons; only patients with moderately (or greater) increased activity in their serum showed positive results. In contrast, by radioimmunoassay as little as 1.0 ng of the phosphatase can be detected in serum.

Download Full-text

Stabilization and Preservation of Serum Prostatic Acid Phosphatase Activity

Clinical Chemistry ◽

10.1093/clinchem/11.10.943 ◽

1965 ◽

Vol 11 (10) ◽

pp. 943-950 ◽

Cited By ~ 15

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.

Download Full-text

Acid phosphatase in Gaucher's disease.

Clinical Chemistry ◽

10.1093/clinchem/26.3.371 ◽

1980 ◽

Vol 26 (3) ◽

pp. 371-382 ◽

Cited By ~ 39

Author(s):

D B Robinson ◽

R H Glew

Keyword(s):

Acid Phosphatase ◽

Phosphatase Activity ◽

Acid Phosphatase Activity ◽

Purification And Characterization ◽

Gaucher's Disease ◽

Gaucher’S Disease ◽

Intracellular Location ◽

Increased Activity ◽

Serum Acid Phosphatase

Download Full-text

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

Clinical Chemistry ◽

10.1093/clinchem/41.2.200 ◽

1995 ◽

Vol 41 (2) ◽

pp. 200-203 ◽

Cited By ~ 9

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.

Download Full-text