scholarly journals LOCALIZATION OF ACID PHOSPHATASE ACTIVITY IN HEPATIC LYSOSOMES BY MEANS OF ELECTRON MICROSCOPY

1961 ◽  
Vol 9 (4) ◽  
pp. 773-784 ◽  
Author(s):  
E. Essner ◽  
Alex B. Novikoff
Keyword(s):  
Electron Microscopy ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Human Liver ◽  
Osmium Tetroxide ◽  
Frozen Sections ◽  
Fixed Tissue ◽  
Thin Sections ◽  
Lipofuscin Granules

Samples of liver from untreated rats, from rats infused with unconjugated bilirubin, and from biopsies of human liver were fixed overnight in cold formol-calcium. Frozen sections were stained for acid phosphatase activity by the Gomori lead-glycerophosphate procedure. Small blocks of fixed tissue were also incubated in this medium. These were then treated briefly with osmium tetroxide, dehydrated, and embedded in methacrylate. Thin sections were studied by electron microscopy. The sites of reaction product of acid phosphatase activity as visualized in electron micrographs are consistent with those seen in frozen sections studied by light microscopy. They indicate that the pericanalicular bodies of parenchymatous cells, the large spherical bodies of Kupffer cells, the microbodies appearing after bilirubin infusion and lipofuscin granules belong to the class of cytoplasmic organelles called lysosomes by de Duve.

Intracellular and Extracellular Acid Hydrolase Activity in the Drosophila Melanogaster Ovary

1982 ◽  
Vol 40 ◽  
pp. 242-243
Author(s):  
Lawrence G. Altman ◽  
R. Witkus ◽  
G. M. Vernon
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Osmium Tetroxide ◽  
Uranyl Acetate ◽  
Acid Hydrolase ◽  
Lead Citrate ◽  
Wild Type ◽  
Thin Sections

Ovaries from wild type Drosophila melanogaster were incubated for acid phosphatase activity (pH 5). Following fixation in either 3.0% or 6.0% glutaraldehyde prepared in 0.1M cacodyiate buffer. Post-fixation was done in 1.0% osmium tetroxide and tissues were subjected to a graded series of acetone and infiltrated with Epon-Araldite. Control tissues were incubated without the substrate, in this case Bglycerophosphate. Ultrastructural integrity was checked against tissue prepared by omitting the incubation period completely. Thin and semi-thin sections were cut on an LKB ultramicrotome. In some instances, observations were recorded without uranyl acetate and lead citrate counterstaining.

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.

Localisation cytochimique des activités phosphatasiques acides de champignons mycorhiziens développés sur milieu complet ou carencé en phosphate

1983 ◽  
Vol 61 (5) ◽  
pp. 1411-1414 ◽  
Author(s):  
Bernadette Lacaze
Keyword(s):  
Electron Microscopy ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Cell Walls ◽  
Acid Phosphatase Activity ◽  
Inorganic Phosphate ◽  
Light And Electron Microscopy ◽  
Reaction Products ◽  
Cytochemical Study

The mycelia of three mycorrhizal basidiomycètes (Pisolithus tinctorius (Pers.) Coker et Couch., Suillus granulatus (L. ex Fr.) O. Kuntze and S. bellinii (Izenga) Watling) were grown on media with or without inorganic phosphate. A cytochemical study of the distribution of acid phosphatase activity was made using light and electron microscopy. Highly enhanced enzyme activity was observed in the phosphorus-deficient mycelia. Precipitates were located primarily at the surface of the fungal cells. Cell walls appear devoid of reaction products in most cases.

scholarly journals CENTRIFUGAL, BIOCHEMICAL, AND ELECTRON MICROSCOPIC ANALYSIS OF CYTOPLASMIC PARTICULATES IN LIVER HOMOGENATES

1956 ◽  
Vol 2 (1) ◽  
pp. 33-54 ◽  
Author(s):  
Edward L. Kuff ◽  
George H. Hogeboom ◽  
Albert J. Dalton
Keyword(s):  
Electron Microscopy ◽  
Acid Phosphatase ◽  
Cytochrome C ◽  
Size Distribution ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Reductase Activity ◽  
Size Group ◽  
Average Radius ◽  
Electron Microscopic

A combined centrifugal, biochemical, and electron microscopic study of the cytoplasmic particulates present in 0.88 M sucrose homogenates of rat liver has been carried out. Size distribution analyses of particles containing pentose nucleic acid (PNA) and exhibiting several types of enzymatic activity revealed three major size groups within the range of particle radius between 10 and 500 mµ. A different array of biochemical properties was associated with each size group. The largest particles, with an average radius (assuming spherical shape) in the region of 220 to 260 mµ, contained all of the succinic dehydrogenase activity of the cytoplasmic extract, 29 per cent of the diphosphopyridine nucleotide (DPN)-cytochrome c reductase activity, and minor amounts of PNA and acid phosphatase activity. Cytologically, this group of particles was identified with the mitochondria. All of the uricase activity, 58 per cent of the acid phosphatase activity, and 26 per cent of the PNA was apparently associated with a second size group of particles (average radius 120 mµ) which were tentatively identified by electron microscopy with vesicular structures derived from the ergastoplasm of the intact cell. The third particle group demonstrated by centrifugation exhibited a major size distribution peak at 25 mµ and a second smaller peak at 55 mµ. Over 50 per cent of the total cytoplasmic PNA and DPN-cytochrome c reductase activity was associated with particles in this size group. Electron microscopy revealed a morphologically heterogeneous population of particles within this size range.

scholarly journals The Localization of Acid Phosphatase in the Sieve Element of Pisum

1969 ◽  
Vol 22 (4) ◽  
pp. 1051 ◽  
Author(s):  
S-Y Zee
Keyword(s):  
Electron Microscopy ◽  
Acid Phosphatase ◽  
Light Microscopy ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Lead Nitrate ◽  
Sieve Tube ◽  
Sieve Element ◽  
Recent Advances ◽  
Acid Phosphatase Reaction

Acid phosphatase activity has been detected within the sieve-tube members of plants by many workers using the Gomori technique and light microscopy (Lester and Evert 1965; Flinn and Smith 1967). Unfortunately the limited resolution makes it difficult to determine the specific sites of activity of the reaction product of the enzyme; recent advances in histochemical techniques for electron microscopy have made it possible to investigate more specifically the sites of localization of the acid phosphatase reaction product by using the Gomori lead nitrate technique (Goldfischer, Essner, and Novikoff 1964; Catesson and Czanenski 1967; Bowen 1968; Figier 1968; Wardrop 1968).

Modifications to the Gomori Acid Phosphatase Technique for Controlled-Temperature Frozen Sections

1963 ◽  
Vol s3-104 (66) ◽  
pp. 193-196
Author(s):  
LUCILLE BITENSKY
Keyword(s):  
Aqueous Solution ◽  
Acetic Acid ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Medium ◽  
Hydrogen Sulphide ◽  
Acid Phosphatase Activity ◽  
Distilled Water ◽  
Frozen Sections ◽  
Tissue Sections

The preservation of inert lysosomes in tissue sections depends on the use of the controlled-temperature freezing-sectioning technique. The Gomori procedure for acid phosphatase produces considerable disintegration of these unfixed sections. This disintegration is not due to incubation in the acid medium nor to the rinsing either in dilute acetic acid or in distilled water, but to the treatment with the solution of ammonium sulphide. It is suggested that for this solution there should be substituted a saturated aqueous solution of hydrogen sulphide gas, which does not cause such cellular deformation. Another improvement involves the deletion of the rinse in acetic acid, because this might render soluble some of the specific precipitate in sections showing minimal acid phosphatase activity.

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