THE DETERMINATION OF URINARY ACID PHOSPHATASES

1952 ◽  
Vol 30 (1) ◽  
pp. 1-9
Author(s):  
G. E. Delory ◽  
Merle Hetherington
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Convenient Method ◽  
Acid Phosphatase Activity ◽  
Acid Phosphatases ◽  
Urinary Acid

The effect of dilution on the apparent acid phosphatase activity of undialyzed and dialyzed urine has been studied. In the former case, the apparent activity increases with dilution but this anomaly is removed by a preliminary dialysis. A convenient method for the determination of acid phosphatase based on this observation is described.

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

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.

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.

Determination of Serum Acid Phosphatase Activity: A Performance Evaluation for Clinical Laboratories of Upstate New York

1972 ◽  
Vol 18 (2) ◽  
pp. 131-136 ◽  
Author(s):  
William H Copeland ◽  
Raymond E Vanderlinde
Keyword(s):  
New York ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
New York State ◽  
Clinical Laboratories ◽  
Normal Ranges ◽  
Target Values ◽  
Definition Of

Abstract Determination of acid phosphatase activity in clinical laboratories in New York State was evaluated. After the target values were established by 12 reference laboratories, sets of test samples were mailed over a two-year period on three occasions to, respectively, 264, 242, and 239 laboratories. Their initial (1968) results revealed problems: definition of normal ranges, interchange of specimens, standardization and quality control, and a need for improved techniques. Almost 5% of laboratories interchanged the initial specimens. Unexpectedly, laboratories using the same method reported a two-fold or greater variation in their "normal range." Although there was some improvement after refresher training sessions, performance was more clearly improved a year later for five of the seven major methods used. Use of the Bessey—Lowry—Brock, Babson—Phillips, and Shinowara—Jones—Reinhart methods resulted in the lowest coefficients of variation.

Trichomonas vaginalis: Determination of Acid Phosphatase Activity as a Pharmacological Screening Procedure

2003 ◽  
Vol 89 (5) ◽  
pp. 1076-1077 ◽  
Author(s):  
M. M. Martínez-Grueiro ◽  
D. Montero-Pereira ◽  
C. Giménez-Pardo ◽  
J. J. Nogal-Ruiz ◽  
J. A. Escario ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Trichomonas Vaginalis ◽  
Screening Procedure ◽  
Pharmacological Screening

GENETIC STUDIES OF ISOZYMES IN NEUROSPORA. I. A STUDY OF EIGHT SPECIES

1971 ◽  
Vol 13 (2) ◽  
pp. 298-305 ◽  
Author(s):  
M. Mohan Reddy ◽  
S. F. H. Threlkeld
Keyword(s):  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Phosphatase Activity ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Starch Gel Electrophoresis ◽  
Acid Phosphatases ◽  
Genetic Studies ◽  
Starch Gel

Mycelial extracts of 34 strains representing eight species of the genus Neurospora were subjected to acrylamide and starch gel electrophoresis to detect sites of esterase, lactate dehydrogenase, amylase, peroxidase, and acid phosphatase activity. Nine isozymes of esterases, four isozymes of lactate dehyrogenases, three isozymes of peroxidases, and two isozymes of acid phosphatases were detected on the gels for the species. The application of zymograms as a biochemical means to characterize species is discussed.

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