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 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.

Phosphatase Activity of Drosophila Salivary Glands

1948 ◽  
Vol s3-89 (8) ◽  
pp. 415-419
Author(s):  
W. L. DOYLE
Keyword(s):  
Acid Phosphatase ◽  
Enzymatic Activity ◽  
Quantitative Determination ◽  
Salivary Glands ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
The State ◽  
Staining Methods

The phosphatases in the cytoplasm and nuclei of Drosophila salivary glands are better preserved by fixation in absolute acetone than in 85 per cent, alcohol. In whole glands there is relatively little extraction of the enzyme during assay. Phosphatase activity is more resistant to incubation at neutrality than at pH 8.6, but in this material there is sufficient residual enzymatic activity to permit redetermination of alkaline, neutral, or acid phosphatase activity by staining methods after an initial quantitative determination. The state of the membranes of the gland affects the penetration of the substrate sufficiently to limit the activities obtained.

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.

Pituitary adrenal interactions in shorn sheep exposed to cold, wet conditions

1969 ◽  
Vol 20 (1) ◽  
pp. 99 ◽  
Author(s):  
BA Panaretto ◽  
KA Ferguson
Keyword(s):  
Acid Phosphatase ◽  
Enzymatic Activity ◽  
Phosphatase Activity ◽  
Cold Exposure ◽  
Acid Phosphatase Activity ◽  
Adrenal Glands ◽  
Adrenocortical Insufficiency ◽  
Acth Stimulation ◽  
Glucuronidase Activity ◽  
Exposure Levels

Newly shorn sheep were exposed to a cold (3°C) wet environment for 8 days; six out of 10 untreated animals died but there were no deaths in a group of 10 that was treated with cortisone. In two other experiments, nine out of 15 control sheep died, but only four out of 15 sheep treated with adrenocorticotrophin (ACTH). In a final experiment approximately one-third of exposed controls died compared with one-tenth of sheep treated with dexamethasone trimethylacetate. A significantly greater proportion (P < 0.05) of sheep given ACTH or 1.5 mg or more of dexamethasone trimethylacetate per kg had rectal temperatures higher than 37.8°C during the first 96 hr of exposure than the comparable controls. The adrenal glands of sheep that died in the cortisone and ACTH experiments were heavier than those taken from survivors that were killed after the experiment; macroscopically, the cortices of some of the adrenals from sheep that succumbed were haemorrhagic and resembled the glands seen in the Waterhouse-Friderichsen syndrome in man; all were heavily infiltrated with lipid when compared with the cortices of survivors. ß-Glucuronidase activity in the serum of cortisone-treated sheep (and in untreated survivors) was elevated during the first 2–3 days of exposure and returned to pre-exposure levels; untreated sheep that succumbed showed continuously increasing enzymatic activity. Acid phosphatase activity was initially depressed in steroid-treated sheep and returned to pre-exposure levels, whereas activity increased continuously in controls that died. Total leucocytes were lower during the first 72 hr of exposure in sheep treated with 1.5–2 mg dexamethasone trimethylacetate per kg, compared with untreated controls. We suggest that the enlarged, fat-laden haemorrhagic adrenals found in sheep that died from cold exposure resulted from excessive ACTH stimulation prior to death. The results suggested a state of adrenocortical insufficiency during the first 96 hr of cold exposure.

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 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.

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.

PHOSPHOMONOESTERASE ACTIVITY IN THE LIFE-CYCLE STAGES OF SCHISTOCERCA GREGARIA

1968 ◽  
Vol 100 (6) ◽  
pp. 649-655 ◽  
Author(s):  
S. N. H. Naqvi ◽  
Shahid H. Ashrafi ◽  
M. A. H. Qadri
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Embryonic Development ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Schistocerca Gregaria ◽  
Adult Males ◽  
First Instar ◽  
Almost All

AbstractThe acid and alkaline phosphatase activity was measured in the developing egg and in the alimentary canal of aging nymphs as well as adult males and females of different ages. Para-nitrophenol was used as colorimetric standard and disodium p-nitrophenyl phosphate as substrate. Activity was measured in terms of micromoles of p-nitrophenol liberated from the substrate as a result of enzyme action.Acid phosphatase activity was noticed to increase with the embryonic development and was higher than in the case of alkaline phosphatase. The alkaline phosphatase activity was lowest in the freshly laid egg, but increased more sharply than acid phosphatase during embryonic development.The activity of both the acid and alkaline phosphatases was highest in the first instar and declined gradually to the fifth instar. The activity of acid phosphatase was higher than alkaline phosphatase in all stages except the first instar where it was almost equal. The activity of both the enzymes was higher during the intermoulting period and declined at each moult indicating a hormone–enzyme relationship.In adults, activity of both the enzymes increased up to the maturation period after which the activity gradually decreased. Acid phosphatase activity was generally higher in males whereas alkaline phosphatase activity was generally higher in females. In almost all cases, the acid phosphatase activity was found to be higher than the alkaline phosphatase.

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