X-ray microanalysis of colloidal-gold-labelled lysosomes in rat liver sinusoidal cells after incubation for acid phosphatase activity

1980 ◽  
Vol 66 (2) ◽  
pp. 137-148 ◽  
Author(s):  
W. C. de Bruijn ◽  
J. P. M. Schellens ◽  
J. M. H. van Buitenen ◽  
J. van der Meulen
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Rat Liver ◽  
Colloidal Gold ◽  
Acid Phosphatase Activity ◽  
Sinusoidal Cells ◽  
X Ray ◽  
Liver Sinusoidal Cells

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.

scholarly journals Microendocytosis in eosinophilic leukocytes.

1975 ◽  
Vol 64 (3) ◽  
pp. 622-635 ◽  
Author(s):  
A Komiyama ◽  
S S Spicer
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Colloidal Gold ◽  
Acid Phosphatase Activity ◽  
Structural Changes ◽  
Fetal Calf Serum ◽  
Calf Serum ◽  
Moderate Activity ◽  
Intraperitoneal Infusion ◽  
Phosphate Buffered Saline

Rat peritoneal eosinophils were examined after intraperitoneal infusion either of a mixture of phosphate-buffered saline (PBS) and colloidal gold or of fetal calf serum. These cells characteristically contained vesiculotubular structures, cuplike structures, and small granules during centrifugation. The cup-shaped structures and elaborate labyrinths of vacuole-like spaces increased markedly after injection of the PBS-colloidal gold mixture, presumably as features of heightened microendocytic activity. The vesiculotubular structures increased greatly after infusion of fetal calf serum. A few cyrstalloid granules exhibited fine-structural changes after the PBS-colloidal gold injection, and more numerous crystalloid granules appeared altered after fetal calf serum. Infrequent small granules contained a lucent, crystal-like silhouette after the fetal calf serum injection. Eosinophils evidenced microendocytic uptake of gold spherules into coated vesicles, the cup-shaped structures, and the small granules, but not into the vesiculotubular structures or crystalloid granules after intraperitoneal infusion of the PBS-gold mixture. Strong unmasked acid phosphatase activity in small granules contrasted with the general lack of activity in normal-appearing crystalloid granules and moderate activity in apparently altered crystalloid granules, presumably reflecting active and latent forms of enzyme in the different granules.

scholarly journals PURIFICATION OF GLUTARALDEHYDE ITS SIGNIFICANCE FOR PRESERVATION OF ACID PHOSPHATASE ACTIVITY

1968 ◽  
Vol 16 (3) ◽  
pp. 199-204 ◽  
Author(s):  
H. DARIUSH FAHIMI ◽  
PIERRE DROCHMANS ◽  
A. POPOWSKI
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Enzymatic Activity ◽  
Phosphatase Activity ◽  
Rat Liver ◽  
Acid Phosphatase Activity ◽  
High Concentration ◽  
Liver Homogenates ◽  
Inorganic Phosphates

The inhibition of acid phosphatase activity in rat liver homogenates after fixation in different lots of commercial glutaraldehyde is determined and compared with the inhibition following fixation with a distilled product. It is shown that commercial glutaraldehydes inhibit more of the enzyme activity than the distilled product. The acidic products of oxidation of glutaraldehyde do not increase the inhibition of the enzymatic activity. The presence of high concentration of inorganic phosphates in different lots of commercial glutaraldehyde, as presented here, suggests that probably such impurities may be responsible for increased inhibition of phosphatase activity noted after fixation in commercial glutaraldehydes.

Changes in acid phosphatase activity in rat liver after ischemia

1989 ◽  
Vol 93 (2) ◽  
pp. 161-166 ◽  
Author(s):  
W. M. Frederiks ◽  
F. Marx
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Rat Liver ◽  
Acid Phosphatase Activity

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.

Aqueous extract of Securidaca longepedunculata root induce redox imbalance in male rat liver and kidney

2010 ◽  
Vol 29 (8) ◽  
pp. 679-688 ◽  
Author(s):  
TO Ajiboye ◽  
AK Salau ◽  
MT Yakubu ◽  
AT Oladiji ◽  
MA Akanji ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Rat Liver ◽  
Aqueous Extract ◽  
Acid Phosphatase Activity ◽  
Male Rat ◽  
Antioxidant Systems ◽  
Liver And Kidney ◽  
Securidaca Longepedunculata ◽  
Serum Acid Phosphatase

The effect of aqueous extract of Securidaca longepedunculata root on redox homeostasis in male rat liver and kidney was investigated. Rats were grouped into four: A, B, C and D, where A (the control) received orally 1 mL of distilled water; B, C and D (test groups) received orally 200, 400 and 800 mg/kg body weight of the extract, respectively, for 28 days. Extract administration significantly reduced (p < .05) alkaline phosphatase activity in the liver and kidney with corresponding increases in the serum. Acid phosphatase activity increased significantly (p < .05) in the liver and kidney, while there was no significant change (p > .05) in the serum acid phosphatase activity. There was also significant decrease (p < .05) in the activities of superoxide dismutase, catalase, glutathione peroxidase and glutathione reductase in the liver and kidney. Liver and kidney levels of GSH, vitamins C and E were also significantly reduced (p < .05). Serum malonidialdehyde and lipid hydroperoxide increased significantly (p < .05) in all the extract-treated groups. The available data from this study revealed that aqueous extract of S. longepedunculata root exerted its toxicity in the animals by depleting the antioxidant systems. This may consequently expose the cells and cellular macromolecules to oxidative damage by reactive oxygen species generated either from the metabolism of the extract or other in vivo means.

Sign in / Sign up

Export Citation Format

Share Document