scholarly journals FINE STRUCTURAL LOCALIZATION OF ACID AND ALKALINE PHOSPHATASES IN CELLS OF RABBIT BLOOD AND BONE MARROW

1967 ◽  
Vol 15 (6) ◽  
pp. 311-334 ◽  
Author(s):  
B. K. WETZEL ◽  
S. S. SPICER ◽  
R. G. HORN
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Mononuclear Cells ◽  
Nuclear Staining ◽  
Alkaline Phosphatases ◽  
Structural Localization ◽  
Dense Granules ◽  
Dense Bodies

In rabbit heterophils, acid phosphatase activity occurs in primary (azurophil) granules which predominate in early cells and persist in mature cells and in tertiary granules which are seen only in mature cells. Alkaline phosphatase activity occurs in secondary granules which appear in intermediate heterophils and later predominate in mature cells. Acid phosphatase activity in heterophil Golgi zones coincides developmentally with the genesis of primary and, later, tertiary granules, whereas alkaline phosphatase in the Golgi complex coincides with secondary granulogenesis. In developing eosinophils, acid phosphatase reaction product occurs in Golgi elements, rims the spherical precursors of angular, mature granules and appears inconsistently within mature granules. Basophil myelocytes show acid phosphatase in Golgi elements but not in specific granules. Additional acid phosphatase reactive structures include: granules of mononuclear cells; phagocytic vacuoles in macrophages; autophagic vacuoles in maturing erythroid cells; small dense granules of platelets; dense bodies in lipocytes; and Golgi elements of mononuclear cells, macrophages, nucleated red cells, megakaryocytes and lipocytes. Localized deposits were absent in control specimens except for enzyme-independent nuclear staining in alkaline phosphatase preparations.

Acid and alkaline phosphatases in the lymphomyeloid tissues of elasmobranch fish

1978 ◽  
Vol 58 (3) ◽  
pp. 727-730 ◽  
Author(s):  
Ragnar Fänge
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
High Activity ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Alkaline Phosphatases ◽  
Large Numbers ◽  
Alkaline Reaction ◽  
Elasmobranch Fish ◽  
Very High

Activities of phosphomonoesterases were measured at acid and at alkaline reaction (pH 4–5 or 9–65) in homogenates of elasmobranch tissues especially lymphomyeloid structures. The animals were dogfish (Scyliorhinus caniculd) and two species of ray (Raja brachyura, R. naevus). Acid phosphatase activity was high in the epigonal tissue, Leydig's organ, the spleen and the thymus. High activity was also found in the pancreas and the kidney, whereas skeletal and cardiac muscle showed low values. The activity of alkaline phosphatase was very high in the kidney and relatively low in other tissues. Ultrasonification of homogenates from the dogfish resulted in increase of acid phosphatase activity but had little effect on alkaline phosphatase activity. The high activity of acid phosphatase in lymphomyeloid tissue may be due to the presence of large numbers of various types of leucocytes.

scholarly journals THE FINE STRUCTURAL LOCALIZATION OF ALKALINE AND ACID PHOSPHATASE ACTIVITY IN THE RAT SUBMANDIBULAR GLAND

1968 ◽  
Vol 16 (9) ◽  
pp. 572-581 ◽  
Author(s):  
BRUCE I. BOGART
Keyword(s):  
Alkaline Phosphatase ◽  
Plasma Membrane ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Myoepithelial Cell ◽  
Structural Localization ◽  
Pinocytotic Vesicles ◽  
Rat Submandibular Gland

The lead capture method was employed to study the fine structural localization of nonspecific phosphatase activity in the rat submandibular gland. Alkaline phosphatase activity was observed in association with the plasma membrane and pinocytotic vesicles of the myoepithelial cell. A polarity in the distribution of alkaline phosphatase activity was described along the myoepithelial cell process. More reaction product was observed in association with the plasma membrane on the parenchymal surface than on the plamsa membrane on the stromal surface, where reaction product was confined mostly to the pinocytotic vesicles. Activity was evenly distributed over both surfaces of the portion of the myoepithelial cell characterized by the nucleus. Activity was also observed to be associated with pinocytotic vesicles of the endothelial cells and the plasma membrane of erythrocytes. No activity was observed in association with the ductal elements. Acid phosphatase activity was associated with membrane-bound structures in the acini and ducts. These structures took the form of lipofuscin granules in the acini and either multivesicular or dense bodies in the ducts.

Acid phosphatase, alkaline phosphatase, and nitrate reductase activity of selected ectomycorrhizal fungi

1989 ◽  
Vol 67 (3) ◽  
pp. 750-753 ◽  
Author(s):  
Iwan Ho
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Nitrate Reductase ◽  
Phosphatase Activity ◽  
Ectomycorrhizal Fungi ◽  
Acid Phosphatase Activity ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Phosphatase Alkaline

Seventeen isolates, encompassing five genera and eight species of ectomycorrhizal fungi, were compared for acid phosphatase, alkaline phosphatase, and nitrate reductase activity. Isolates within species differed in enzyme activity and isozyme patterns by host specificity and site (as exemplified by the genus Suillus). Host and site may have affected phosphatase enzyme activity. Generally, the Douglas-fir associates, which dominate in mesic sites, have higher acid phosphatase activity than pine associates, which mostly occupy xeric sites; however, pine associates from mesic sites also have higher acid phosphatase activity (e.g., S. tomentosus). In four isolates of Amanita muscaria, the effect of site was also apparent. Two of them, which have significantly higher acid phosphatase activity than the others, were isolated from mesic sites. The isozyme pattern of the genus Suillus appeared to be separated by host groups. Other isolates with only one species also differed more or less by host groups. They shared at least one band within host groups, except for the two isolates of Paxillus involutus from different hosts. The P. involutus S-403 isolated from an orchard showed much higher nitrate reductase activity than all other isolates. No apparent differences in nitrate reductase activity were found between the other isolates.

scholarly journals The effect of different copper doses and organic fertilisation on soil’s enzymatic activity

2020 ◽  
Vol 66 (No. 2) ◽  
pp. 93-98
Author(s):  
Beata Kuziemska ◽  
Andrzej Wysokiński ◽  
Joanna Trębicka
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Enzymatic Activity ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Organic Materials ◽  
Chicken Manure ◽  
Test Plant ◽  
Orchard Grass ◽  
Organic Fertilisation

A three-year pot experiment carried out in the vegetation hall in 2014–2016 included studying the enzymatic activity of soil, into which various amounts of copper: (100, 200 and 300 mg Cu/kg soil) and organic materials (cattle manure, chicken manure, post-mushroom substrate) were introduced, used separately, at a soil-introduction dose of 2 g C<sub>org</sub>/kg. Copper and organic materials were used once, only in the first year of the study, before sowing test plant orchard grass. In soil collected after the last (fourth) swath of grass in each year of the study, the activity of urease, dehydrogenases, acid, and alkaline phosphatase was determined. Applications of copper to the soil, regardless of its dose, resulted in a decrease in urease, dehydrogenases and alkaline phosphatase and an increase in acid phosphatase activity. The inactivating effect of this metal on the activity of urease, dehydrogenases and alkaline phosphatase increased with the increase of its dose. Organic fertilisation generally increased the enzymatic activity of the analysed soil. In subsequent years of the study, urease and alkaline phosphatase activity decreased, while acid phosphatase activity increased. Dehydrogenase activity did not change significantly in subsequent years of the study.  

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.

scholarly journals DISTRIBUTION OF PHOSPHATASES IN THE GOLGI REGION AND ASSOCIATED STRUCTURES OF THE THORACIC GANGLIONIC NEURONS IN THE GRASSHOPPER, MELANOPLUS DIFFERENTIALIS

1968 ◽  
Vol 37 (1) ◽  
pp. 89-104 ◽  
Author(s):  
Nancy J. Lane
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Spatial Association ◽  
Thiamine Pyrophosphate ◽  
Multivesicular Bodies ◽  
Dense Bodies ◽  
Developmental Relationship ◽  
Golgi Region ◽  
Melanoplus Differentialis

The neuronal perikarya of the grasshopper contain sudanophilic lipochondria which exhibit an affinity for vital dyes. These lipochondria are membrane-delimited and display acid phosphatase activity; hence they correspond to lysosomes. Unlike those of most vertebrates, these lysosomes also hydrolyze thiamine pyrophosphate and adenosine triphosphate. Like vertebrate lysosomal "dense bodies," they are electron-opaque and contain granular, vesicular, or lamellar material. Along with several types of smaller dense bodies, they are found in close spatial association with the Golgi apparatus. The Golgi complexes are frequently arranged in concentric configurations within which these dense bodies lie. Some of the smaller dense bodies often lie close to or in association with the periphery of dense multivesicular bodies. Further, bodies occur that display gradations in structure between these multivesicular bodies and the dense lysosomes. Acid phosphatase activity is present in the small as well as the larger dense bodies, in the multivesicular bodies, and in some of the Golgi saccules, associated vesicles, and fenestrated membranes; thiamine pyrophosphatase is found in both the dense bodies and parts of the Golgi complex. The close spatial association of these organelles, together with their enzymatic similarities, suggests the existence of a functional or developmental relationship between them.

Soil enzyme activities following paper sludge addition in a winter cabbage-sweet corn rotation

2000 ◽  
Vol 80 (1) ◽  
pp. 91-97 ◽  
Author(s):  
B. Gagnon ◽  
R. Lalande ◽  
R. R. Simard ◽  
M. Roy
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Sweet Corn ◽  
Soil Enzyme ◽  
Phosphatase Activities ◽  
Arylsulfatase Activity ◽  
Papermill Sludge ◽  
Soil Acid Phosphatase

Combined primary and secondary papermill sludge (PS) is a good source of C and other nutrients for soils devoted to intensive horticultural production. A field study was conducted to evaluate the effect of PS, spring-applied alone or in combination with ammonium nitrate (AN), on the enzymatic activity of a Bedford clay (Humic Gleysol) in the province of Québec, Canada. The experiment was started in 1996 with winter cabbage (Brassica oleracea var. capitata L.) and continued in 1997 and 1998 on the same plots with sweet corn (Zea mays L.). The PS was applied at 0 (control), 8, 16, 32 and 65 Mg ha−1 in 1996 and at 44% of these rates in 1997. No sludge was applied in 1998. Additional treatments consisted of AN applied yearly at 100% of the plant N requirements and a PS and AN combination. Soil arylsulfatase and acid and alkaline phosphatase activities were measured at three different times in each growing season. The PS rate linearly increased the soil acid phosphatase activity in all 3 yr. In contrast, the alkaline phosphatase and arylsulfatase activities were enhanced in 1997 by the 8–16 Mg PS ha−1 treatments, whereas larger amounts of PS showed activity comparable to the control. The second PS application promoted phosphatase activities mostly in fall, but did not sustain arylsulfatase activity. The AN gave lower phosphatase activities than PS, and depressed arylsulfatase. Addition of AN to PS increased only acid phosphatase activity as compared with PS alone or the control. This study indicated that addition of PS improved enzyme activity of this horticultural soil but rates in excess to 32 Mg ha−1 may be detrimental. Key words: Papermill sludge, soil enzyme, cabbage, corn

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.

Studies on Leukocyte Phosphatases. III. Inhibition of Leukocyte Acid Phosphatase by Zinc

1971 ◽  
Vol 17 (12) ◽  
pp. 1176-1179 ◽  
Author(s):  
Lawrence R DeChatelet ◽  
M Robert Cooper ◽  
Charles E McCall
Keyword(s):  
Amino Acids ◽  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Leukocyte Alkaline Phosphatase

Abstract Whereas the activity of leukocyte alkaline phosphatase is stimulated by Zn2+, it inhibits acid phosphatase activity. The degree of inhibition of acid phosphatase depends on the pH of the medium, being greater as the pH approaches neutrality. This inhibition may be at least partially reversed by the addition of amino acids, which suggests that interactions of Zn2+ and amino acids may play an important role in regulating the overall phosphatase activity of the leukocyte.

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