An X-ray microanalytical azo dye technique for the localization of acid phosphatase activity

1976 ◽  
Vol 49 (1) ◽  
pp. 43-50 ◽  
Author(s):  
Ivor D. Bowen ◽  
Timothy A. Ryder ◽  
Nerys L. Downing
1959 ◽  
Vol 7 (1) ◽  
pp. 39-41 ◽  
Author(s):  
M. S. BURSTONE

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.


1982 ◽  
Vol 30 (1) ◽  
pp. 86-90 ◽  
Author(s):  
J P Berry ◽  
J Hourdry ◽  
M Sternberg ◽  
P Galle

A new method is described that demonstrates acid phosphatase activity in the cells of the proximal tubules of the rat kidney. The method is based on the formation of an insoluble aluminum phosphate precipitate. Microanalysis was used to demonstrate the presence of intracellular aluminum and determine the quantity present under the probe. Parallel biochemical studies showed that the aluminum precipitate was indeed due to acid phosphatase activity.


1966 ◽  
Vol 14 (2) ◽  
pp. 171-176 ◽  
Author(s):  
G. W. EVANS ◽  
CECILIA L. WHINNEY ◽  
K. C. TSOU

5-Iodoindoxyl phosphate has been found to be a useful indigogenic substrate in the histochemical demonstration of acid phosphatase activity. Its superiority to other indoxyl phosphates is apparently due to a rapid oxidation of 5-iodoindoxyl to 5,5'-diiodoindigo in the acid pH range. A redox system of ferri-ferrocyanide enhances the oxidation and improves the localization. This method can be applied to calcium-formol-fixed tissues or to fresh frozen sections, although fixed tissues yield better results. The method is not recommended for the demonstration of enzyme activity in lipid-rich tissues because of the complexing property of lipids with 5,5'-diiodoindigo that results in crystal formation. The distribution of acid phosphatase activity with this method is generally similar to that obtained using azo dye methods.


1966 ◽  
Vol 44 (6) ◽  
pp. 755-761 ◽  
Author(s):  
John P. Manning ◽  
Arthur L. Babson ◽  
Margaret C. Butler ◽  
Sara F. Priester

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.


1987 ◽  
Vol 87 (1) ◽  
pp. 71-77 ◽  
Author(s):  
J. B. van Dorf ◽  
J. Ph. Zeelen ◽  
W. C. de Bruijn

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