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.

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.

Acid phosphatase in Gaucher's disease.

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.

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

Serum acid phosphatase activity in the diagnosis of carcinoma of the prostate

Pathology ◽  
1977 ◽  
Vol 9 (1) ◽  
pp. 85
Author(s):  
R.D. McEvoy ◽  
P.J. Phillips ◽  
R. Rowland ◽  
J.-B. Edwards ◽  
R. Bais
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Carcinoma Of The Prostate ◽  
Serum Acid Phosphatase
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