scholarly journals Amino Acid Phosphatase Activity of Alkaline Phosphatase. A Possible Role of Protein Phosphatase

1995 ◽  
Vol 227 (1-2) ◽  
pp. 367-371 ◽  
Author(s):  
Tetsuya Shinozaki ◽  
Hideomi Watanabe ◽  
Satoru Arita ◽  
Masaki Chigira
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Amino Acid ◽  
Phosphatase Activity ◽  
Protein Phosphatase ◽  
Acid Phosphatase Activity

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.  

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 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.

Role of enzymes in the mechanism of shell penetration by the muricid gastropod, Thais lapillus (L.)

1977 ◽  
Vol 55 (11) ◽  
pp. 1846-1857 ◽  
Author(s):  
Roy S. Webb ◽  
A. S. M. Saleuddin
Keyword(s):  
Acid Phosphatase ◽  
Carbonic Anhydrase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Carbonic Anhydrase Activity ◽  
Marker Enzyme ◽  
Biochemical Activity ◽  
Significant Difference ◽  
Muricid Gastropods

The role of the boring organ in the mechanism of shell penetration by Thais lapillus (L.), a muricid gastropod, has been investigated by cytochemistry and biochemistry. Sites of acid phosphatase and carbonic anhydrase activity were localized and the biochemical activities of these enzymes were measured in the boring organ of both nonboring and actively boring animals. The lysosomal marker enzyme, acid phosphatase, was investigated to assess the role of lysosomes in the boring mechanism. Acid phosphatase activity was localized on the microvillar membranes of the epithelial cells of the boring organ. There was no significant difference in the biochemical activity of acid phosphatase between actively boring and nonboring specimens. Carbonic anhydrase was localized prominently in the epithelium of the boring organ. The microvilli showed no localization but all other regions of the epithelium were dominated by reaction product. The boring organ demonstrated high levels of carbonic anhydrase activity but no significant difference could be detected between actively boring and nonboring specimens. The possible involvement of these enzymes and their role in the mechanism of shell penetration by muricid gastropods has been discussed.

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

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.

Intraspecific genetic variation of acid phosphatase activity in monokaryotic and dikaryotic populations of the ectomycorrhizal fungus Hebeloma cylindrosporum

1991 ◽  
Vol 69 (4) ◽  
pp. 808-813 ◽  
Author(s):  
J. P. Meysselle ◽  
G. Gay ◽  
J. C. Debaud
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Specific Activity ◽  
Intraspecific Variability ◽  
Ectomycorrhizal Fungus ◽  
Hebeloma Cylindrosporum ◽  
Single Strain ◽  
Wild Strains

Intraspecific variability of acid phosphatase activity and mycelial growth of the ectomycorrhizal fungus Hebeloma cylindrosporum Romagnesi was examined because of the role of this enzyme activity in the phosphate nutrition of the fungus and consequently of mycorrhizal host plants. Interstrain variation was studied with 11 wild strains, and intrastrain variability was studied with 20 sib-monokaryons and 50 reconstituted dikaryons, progeny of the HC1 fruiting strain. The range of variation of acid phosphatase activity among wild dikaryotic mycelia was the same as that among sib-monokaryons or dikaryons belonging to the progeny of a single strain. The total phosphatase activity of the wild strains ranged from 5.70 to 96.0 total milliunits (TmU). It ranged from 11.1 to 120.5 TmU within sib-monokaryons and from 34.2 to 178.1 TmU for reconstituted dikaryons. Specific phosphatase activity of wild dikaryons ranged from 48.5 international milliunits (ImU) to 675.6 ImU, whereas the ranges of variation among sib-monokaryons and reconstituted dikaryons were, respectively, 85.3–791.0 and 270.7–816.1 ImU. On average, sib monokaryons and reconstituted dikaryons had lower activity than their parental dikaryon. However, four reconstituted dikaryons had a higher specific activity than the original dikaryon HC1. The growth of the studied mycelia also varied, but in a narrower range (from 97.1 to 151.6 μg protein per culture for wild dikaryons, from 130.1 to 199.1 μg for sib-monokaryons, and from 160.6 to 275.9 μg for reconstituted dikaryons). No correlation could be detected between specific acid phosphatase activity and growth rate in pure culture within the different monokaryotic or dikaryotic populations studied. These results demonstrate the possibility of obtaining, by intrastrain crossings, mycelia having higher phosphatase activity than the parental wild strains. The characteristics of the different mycelia are discussed in relation to a selection program and their putative spatial distribution in natural conditions. Key words: acid phosphatase, ectomycorrhizal fungus, intraspecific variation, monokaryon, dikaryon, Hebeloma cylindrosporum.

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