Some properties of a Ca2+- and (or) Mg2+-requiring nucleoside di- and tri-phosphatase(s) associated with the membranes of rat pancreatic zymogen granules

1978 ◽  
Vol 56 (6) ◽  
pp. 565-576 ◽  
Author(s):  
Francis Harper ◽  
François Lamy ◽  
Raymond Calvert
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Active Site ◽  
Acid Phosphatase Activity ◽  
Plasma Membranes ◽  
Zymogen Granules ◽  
Tentative Conclusion ◽  
Data Support ◽  
Single Protein ◽  
Hydrolysis Of

Membranes of rat pancreatic zymogen granules have been purified and found to be essentially free of contamination by mitochondria, microsomes, and plasma membranes. They possessed an acid phosphatase activity which derived probably from lysed lysosomes contaminating the purified zymogen granules from which the membranes were prepared. These membranes were found to contain a strong Ca2+- and (or) Mg2+-requiring activity toward all nucleoside di- and tri-phosphates. Various data support the tentative conclusion that a single protein catalyzes the hydrolysis of the nucleoside di- and tri-phosphates. This protein appears to be intrinsic with its active site localized on the internal face of the membranes.

Polyphosphate body and acid phosphatase localization in Nostoc sp.

1984 ◽  
Vol 30 (1) ◽  
pp. 8-15 ◽  
Author(s):  
John D. DuBois ◽  
Keith R. Roberts ◽  
Lawrence A. Kapustka
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Energy Stress ◽  
Nitrophenyl Phosphate ◽  
Carbon Compounds ◽  
Electron And Light Microscopy ◽  
Polyphosphate Bodies ◽  
Hydrolysis Of

Polyphosphate bodies and acid phosphatase activity were characterized in Nostoc sp. to determine if the hydrolysis of polyphosphate bodies occurs during dark (energy stress) periods. Electron and light microscopy were used to locate polyphosphate bodies. Acid phosphatase activity was measured using p-nitrophenyl phosphate as the substrate to determine net changes in the level of the enzyme activity. To induce energy stress, Nostoc sp. cells were kept in the dark for 72 h to deplete stored carbon compounds. Cells incubated in the light for 72 h (controls) showed acid phosphatase activity localized around the perimeter of polyphosphate bodies. When cells were incubated in the dark, acid phosphatase activity occurred throughout the polyphosphate body matrix. However, complete hydrolysis of the polyphosphate body did not occur and the rate of acid phosphatase activity was not affected.

The host-parasite interface of Cyathocotyle bushiensis Khan, 1962 (Trematoda: Strigeoidea)

Parasitology ◽  
1968 ◽  
Vol 58 (2) ◽  
pp. 371-375 ◽  
Author(s):  
David A. Erasmus
Keyword(s):  
Electron Microscope ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Plasma Membranes ◽  
Science Research ◽  
Strong Acid ◽  
Gland Cells ◽  
Adhesive Organ ◽  
Cyathocotyle Bushiensis

A combination of histochemical and electron microscope techniques have demonstrated, in Cyathocotyle bushiensis, alkaline phosphatase activity in the matrix of the tegument, in the distal and basal plasma membranes of the tegument, in the wall of the ducts extending from the adhesive organ gland cells and in the wall of the adhesive organ microvilli. Acid phosphatase activity was much stronger and was present in the tegument matrix and in the granular component of the secretion from the adhesive organ gland cells. Strong acid phosphatase activity was also present in the cisternae of the endoplasmic reticulum of the adhesive organ gland cells.I am greatly indebted to Professor Brough for the excellent facilities available within this department. I also wish to thank Professor J. Sinclair (Department of Mining) for electron microscope facilities extended to me in the early stages of this investigation, and to Mr W. Henderson, Mr T. Davies and Miss M. Williams for their invaluable assistance. The purchase of the Huxley ultramicrotome, coating unit and an AEI EM 6 electron microscope was made possible by a grant from the Science Research Council.

QUANTITATIVE STUDIES ON ISOLATED PANCREATIC ISLETS OF MAMMALS: ENZYMIC HYDROLYSIS OF NUCLEOSIDE DIPHOSPHATES AND p-NITROPHENYL PHOSPHATE IN NORMAL AND CORTISONE-TREATED RATS

1966 ◽  
Vol 36 (2) ◽  
pp. 115-NP ◽  
Author(s):  
I.-B. TÄLJEDAL ◽  
B. HELLMAN ◽  
C. HELLERSTRÖM
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Sodium Fluoride ◽  
Acid Phosphatase Activity ◽  
Staining Intensity ◽  
Histochemical Staining ◽  
Enzymic Hydrolysis ◽  
Isolated Pancreatic Islets ◽  
Hydrolysis Of

SUMMARY Chemical micromethods and histochemical staining were employed for studies of the enzymic hydrolysis of inosine diphosphate (IDP) and adenosine diphosphate (ADP) and the non-specific acid phosphatase activity of the endocrine pancreas from normal and cortisone-treated rats. The following observations were made: 1. Enzymic dephosphorylation of IDP and ADP was maximal at about pH 8·0. Magnesium and manganese ions enhanced the phosphate liberation, the hydrolysis of ADP being more activated than that of IDP. A marked inhibition of enzyme activity towards either substrate was produced by sodium fluoride, sodium cyanide and ethylene-diaminotetraacetate. Acid phosphatase activity was maximal at about pH 5·5, a tendency for a second activity optimum was noted at about pH 4·0. Acid phosphatase activity was markedly inhibited by sodium fluoride, tartaric acid and formaldehyde. 2. Histochemical staining revealed marked enzyme activity towards IDP and ADP in the capillaries and walls of the large blood vessels throughout the pancreas, whereas the islet cells displayed a moderate reaction. The staining intensity was the same with IDP as with ADP. 3. Cortisone administration reduced the rate of cleavage of both IDP and ADP in both the endocrine and the exocrine pancreas, but the enzymic splitting of these substrates remained unchanged in the liver. Acid phosphatase activity was not influenced in any of these tissues by the steroid treatment.

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

Tartrate-resistant acid phosphatase activity and glutathione levels are modulated during hFOB 1.19 osteoblastic differentiation

2008 ◽  
Vol 39 (6) ◽  
pp. 627-634 ◽  
Author(s):  
Tatiana Salles de Souza Malaspina ◽  
Célio Xavier dos Santos ◽  
Ana Paula Campanelli ◽  
Francisco Rafael Martins Laurindo ◽  
Mari Cleide Sogayar ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Osteoblastic Differentiation ◽  
Tartrate Resistant Acid Phosphatase
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