scholarly journals An ultrastructural localization of lysosomal acid phosphatase activity in aging mouse spleen: A quantitative X-ray microanalytical study.

1991 ◽  
Vol 24 (2) ◽  
pp. 201-208 ◽  
Author(s):  
M. T. OLEA
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Ultrastructural Localization ◽  
Mouse Spleen ◽  
Lysosomal Acid ◽  
X Ray ◽  
Aging Mouse

scholarly journals Aluminum phosphate visualisation of acid phosphatase activity: a biochemical and x-ray microanalysis study.

1982 ◽  
Vol 30 (1) ◽  
pp. 86-90 ◽  
Author(s):  
J P Berry ◽  
J Hourdry ◽  
M Sternberg ◽  
P Galle
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Rat Kidney ◽  
Aluminum Phosphate ◽  
Proximal Tubules ◽  
New Method ◽  
X Ray ◽  
Biochemical Studies

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.

Acid phosphatase activity in Pinus pinea – Tuber albidum ectomycorrhizal association

1992 ◽  
Vol 70 (7) ◽  
pp. 1377-1383 ◽  
Author(s):  
S. Pasqualini ◽  
F. Panara ◽  
M. Antonielli
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Middle Lamella ◽  
Ultrastructural Localization ◽  
Ectomycorrhizal Fungus ◽  
Pinus Pinea ◽  
Inorganic Pyrophosphate ◽  
Mycorrhizal Roots ◽  
Substrate Concentrations

Acid phosphatase activity of pine (Pinus pinea L.) roots was investigated in the presence or absence of the ectomycorrhizal fungus Tuber albidum Pico. Acid phosphatase activity was higher in mycorrhizal roots than in roots of uncolonized control plants. The optimum pH values for acid phosphatase were 3.5 and 5.0 for mycorrhizal roots and 5.0 for control roots. The acid phosphatase activity was inhibited by tartrate, fluoride, and molybdate ions, but a lower inhibition was exerted by orthophosphate. Mycorrhizal roots of pine possessed active acid phosphatases that hydrolyzed a wide variety of natural and synthetic phosphate esters. In particular, the enzyme was active against phytate and inorganic pyrophosphate. Two different Km values were estimated: about 0.22 mM and 2.78 mM at low and high substrate concentrations, respectively. The ultrastructural localization of acid phosphatase in mycorrhizal roots showed that the activity in the Hartig net was mainly localized in the plasmalemma of hyphae. Some lead phosphate precipitates were also observed in the middle lamella of the host cell. Key words: Pinus pinea, Tuber albidum, acid phosphatase, ectomycorrhiza, histochemical localization.

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
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Azo Dye ◽  
X Ray

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.

ULTRASTRUCTURAL LOCALIZATION OF A CHARACTERISTIC ACID PHOSPHATASE IN GRANULES OF RABBIT BASOPHILS

1974 ◽  
Vol 22 (12) ◽  
pp. 1092-1104 ◽  
Author(s):  
ATSUSHI KOMIYAMA ◽  
SAMUEL S. SPICER
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Potential Role ◽  
Strong Acid ◽  
Ultrastructural Localization ◽  
Buffy Coat ◽  
Cytoplasmic Granules ◽  
Nitrophenyl Phosphate ◽  
Tris Maleate

Bone marrow basophils incubated in Gomori medium at pH 6.0-6.8 exhibited strong acid phosphatase activity suggestive of a potential role in endocytosis in one-third of the cytoplasmic granules and also in Golgi elements. Buffy coat basophils contained about one-third as many reactive granules. Reaction product was confined to the threadlike component of the larger granules predominant in early basophils and was absent from the denser-type granules predominant in late basophils. In centrioles of basophils acid phosphatase appeared localized between triplet fibers. Reactivity with the Gomori medium was diminished at pH 5.0, absent at pH 8.0 and only slightly decreased with p-nitrophenyl phosphate as substrate. Basophils incubated in Barka-Anderson medium at pH 5.0-6.8 revealed light acid phosphatase activity in the Golgi lamellae but essentially none in cytoplasmic granules. Tris-maleate buffer of the Barka-Anderson medium replacing the sodium acetate of the Gomori medium inhibited the reactivity in the granules. Incubation in media containing NaF, or lacking substrate, eliminated the heavy precipitates in granules and Golgi elements but yielded light, nonenzymatic lead staining in Golgi and tubulovesicular structures and atypical granules present only in buffy coat basophils.

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