DETERMINATION OF ACID PHOSPHATASE ACTIVITY IN TISSUE HOMOGENATES

1966 ◽  
Vol 44 (6) ◽  
pp. 755-761 ◽  
Author(s):  
John P. Manning ◽  
Arthur L. Babson ◽  
Margaret C. Butler ◽  
Sara F. Priester
Keyword(s):  
Small Intestine ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Azo Dye ◽  
Accurate Method ◽  
Acid Phosphate ◽  
Fast Red ◽  
Tissue Homogenates

A simple and accurate method is described for the quantitative determination of acid phosphatase in tissue homogenates, utilizing stable buffered sodium α-naphthyl acid phosphate tablets as substrate, and the monocoupler Fast Red Salt B as the color developer. This technique eliminates deproteinization and ethyl acetate extraction, and produces a highly colored blue azo dye for spectrophotometry. Of the rat organs tested, the spleen had the highest acid phosphatase activity, then kidney, small intestine, liver, lung, and heart, in that order.

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

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.

scholarly journals HISTOCHEMICAL DEMONSTRATION OF ACID PHOSPHATASE ACTIVITY IN OSTEOCLASTS

1959 ◽  
Vol 7 (1) ◽  
pp. 39-41 ◽  
Author(s):  
M. S. BURSTONE
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Comparative Studies ◽  
Acid Phosphatase Activity ◽  
Azo Dye ◽  
Histochemical Demonstration ◽  
Accurate Localization ◽  
Acid And Alkaline Phosphatase ◽  
Cold Acetone

High acid phosphatase activity was observed in osteoclasts of several species using a reproducible azo-dye technique. High activity of two distinct enzymes, acid and alkaline phosphatase, are associated with osteoclasts and osteoblasts respectivey. Althouth frozen-dried tissues are recommended for definitive studies, the enzyme techniques used give satisfactory results with cold acetone-fixed tissues. The most accurate localization of acid phosphatase in osteoclasts in controlled comparative studies is obtained with double-embedded frozen-dried undecalcified tissues in conjunction with naphthol AS-phosphates.

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.

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.

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