scholarly journals THE HISTOCHEMICAL DEMONSTRATION OF ACID PHOSPHATASE BY A POST-INCUBATION COUPLING TECHNIQUE

1955 ◽  
Vol 3 (6) ◽  
pp. 455-470 ◽  
Author(s):  
ALEXANDER M. RUTENBURG ◽  
ARNOLD M. SELIGMAN
Keyword(s):  
Acid Phosphatase ◽  
Histochemical Demonstration ◽  
Coupling Technique

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.

Histochemical Demonstration of Leukocytic Acid Phosphatase

1979 ◽  
Vol 72 (5) ◽  
pp. 886.1-886
Author(s):  
William H. Starkweather ◽  
Ronald L. Searcy
Keyword(s):  
Acid Phosphatase ◽  
Histochemical Demonstration

scholarly journals Demonstration of tartrate-resistant acid phosphatase in un-decalcified, glycolmethacrylate-embedded mouse bone: a possible marker for (pre)osteoclast identification.

1986 ◽  
Vol 34 (10) ◽  
pp. 1317-1323 ◽  
Author(s):  
F P van de Wijngaert ◽  
E H Burger
Keyword(s):  
Bone Marrow ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Mononuclear Cells ◽  
Histochemical Demonstration ◽  
Splenic Tissue ◽  
Tartrate Resistant Acid Phosphatase ◽  
Excellent Preservation ◽  
Histochemical Marker

Fixed, undecalcified mouse long bones were embedded in glycol methacrylate (GMA), sectioned, and incubated for acid phosphatase in the presence or absence of tartrate, to investigate the feasibility of tartrate-resistant acid phosphatase as a histochemical marker for osteoclast identification. Naphthol AS-BI phosphate was used as the substrate and hexazonium pararosanaline as coupler. Cytocentrifuge preparations of mouse, rat, and quail bone marrow or frozen and GMA sections of mouse splenic tissue were used as controls to specify acid phosphatase activity. After adequate fixation, acid phosphatase activity sensitive to tartrate inhibition (TS-AP) was demonstrated in macrophages from spleen, bone marrow, and loose connective tissue surrounding bone rudiments. Acid phosphatase activity resistant to tartrate inhibition (TR-AP), was detected in multi-nuclear osteoclasts and in some mononuclear cells from bone marrow and periosteum. In cytocentrifuge preparations and frozen sections of mouse spleen, TR-AP was demonstrated after simultaneous incubation with substrate and tartrate. In GMA sections, however, TR-AP could only be demonstrated after pre-incubation with tartrate before application of substrate. We suggest that histochemical demonstration of TR-AP versus TS-AP on GMA-embedded bone sections by means of a pre-incubation method can be used as an identification marker of (pre)osteoclasts. Plastic embedding is recommended for its excellent preservation of morphology and enzyme activity.

scholarly journals A NEW HISTOCHEMICAL METHOD FOR ACID PHOSPHATASE BY THE USE OF 5-IODOINDOXYL PHOSPHATE

1966 ◽  
Vol 14 (2) ◽  
pp. 171-176 ◽  
Author(s):  
G. W. EVANS ◽  
CECILIA L. WHINNEY ◽  
K. C. TSOU
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Azo Dye ◽  
Redox System ◽  
Histochemical Demonstration ◽  
Crystal Formation ◽  
Frozen Sections ◽  
Fresh Frozen ◽  
Ph Range

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.

scholarly journals HISTOCHEMICAL DEMONSTRATION OF CHANGES IN THE ACTIVITY OF ALKALINE AND ACID PHOSPHATASES IN THE ADRENAL OF A MIGRATORY STARLING

1964 ◽  
Vol 12 (10) ◽  
pp. 772-776 ◽  
Author(s):  
D. V. NAIK ◽  
J. C. GEORGE
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Adrenal Cortex ◽  
Adrenocorticotropic Hormone ◽  
Acid Metabolism ◽  
Histochemical Demonstration ◽  
Nucleic Acid Metabolism ◽  
Acid Phosphatases ◽  
Very High ◽  
Alkaline And Acid Phosphatases

The activity of alkaline and acid Phosphatases was studied in adrenal cortex and medulla at the beginning and the end of the period of preparation for migration in the migratory starling, Sturnus roseus. Alkaline phosphatase in cortex and acid phosphatase in medulla showed very high increases as migration approached. The increase in alkaline phosphatase activity is correlated with increase in adrenocorticotropic hormone, ribonucleic acid, corticoids and fat in adrenal cortex, and the increase in acid phosphatase in adrenal medulla with increase in adrenalin and nor-adrenalin production. The increase in acid phosphatase in the nuclei of the cortical and medullary cells is correlated with increased nucleic acid metabolism.

scholarly journals Quantitative histochemical study of acid phosphatase activity in rat liver using a semipermeable membrane technique.

1987 ◽  
Vol 35 (2) ◽  
pp. 175-180 ◽  
Author(s):  
W M Frederiks ◽  
F Marx ◽  
G N Jonges ◽  
C J Van Noorden
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Rat Liver ◽  
Acid Phosphatase Activity ◽  
Enzyme Inhibitors ◽  
Semipermeable Membrane ◽  
Coupling Technique ◽  
Lysosomal Acid ◽  
Membrane Technique ◽  
Post Coupling

Acid phosphatase activity has been demonstrated in rat liver with the semipermeable membrane technique using naphthol AS-BI phosphate as substrate and hexazotized pararosaniline (HPRA) as simultaneous coupling agent. With this method the final reaction product (FRP) appeared in rat liver as intensely colored red granules in liver parenchymal cells and in Küpffer cells. The absorbance spectrum of the FRP peaks between 510 and 550 nm. A nonspecific reaction product, as has been found in skeletal muscle, did not occur in rat liver. A substrate concentration of 5 mM and a HPRA concentration of 10 mM result in optimum localization and activity. We concluded from the results with different enzyme inhibitors that lysosomal acid phosphatase was demonstrated. The mean absorbance of the FRP increased linearly with incubation time (15-60 min). Furthermore, we found a linear increase of the FRP with increasing section thickness (4-10 micron). When the simultaneous coupling method was replaced by a post-coupling technique, the colored reaction product was diffusely located throughout the cytoplasm. In conclusion, the simultaneous coupling technique in combination with the semipermeable membrane method is a valuable tool for detecting and quantifying lysosomal acid phosphatase activity in rat liver. We demonstrated that acid phosphatase activity is 1.2 times higher periportally than pericentrally in rat liver, and that 24 hr fasting before the experiments did not change the acid phosphatase activity.

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