scholarly journals Response Of Actinomycetes, Phosphatases And Urease To Soil Contamination With Herbicides

2015 ◽  
Vol 22 (2) ◽  
pp. 255-267
Author(s):  
Małgorzata Baćmaga ◽  
Jan Kucharski ◽  
Jadwiga Wyszkowska ◽  
Monika Tomkiel ◽  
Agata Borowik
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Soil Contamination ◽  
Sandy Loam ◽  
Inhibitory Effect ◽  
Colony Development ◽  
Alkaline Phosphatases ◽  
Resilience Index ◽  
Activity Of Enzymes ◽  
Resistance To Herbicides

Abstract A laboratory experiment was completed to determine the effect of the herbicides Alister Grande 190 OD, Fuego 500 SC and Lumax 537.5 SE on counts of actinomycetes as well as the activity of enzymes and their resistance to herbicides. Sandy loam was mixed with appropriate doses of the herbicides, such as: 0 - the control, 1 - technological dose and doses 20-, 40-, 80- and 160-fold higher than recommended. On day 20, 40, 80 and 160, counts of actinomycetes and activity of urease, acid phosphatase and alkaline phosphatase were determined. For 160 days, soil was incubated at 25°C and its moisture content was maintained on a constant level equal 50% of water capillary capacity. On days 20 and 80 of the experiment, the ecophysiological (EP) and colony development (CD) indices were computed. Additionally, the resistance (RS) of enzymes to the herbicides was assessed on day 20 and their resilience index (RL) was determined on day 160. It has been found out that soil contamination with herbicides contributed to elevated counts of actinomycetes. The highest number of these microorganisms was observed in soil with Lumax 537.5 SE, and the lowest one appeared in soil with Alister Grande 190 OD. The CD for actinomycetes was the highest in treatments with Fuego 500 SC and the highest EP was determined in soil with Alister Grande 190 OD. Application of the herbicides in doses from 20- to 160-fold higher than recommended by the manufacturer significantly increased the activity of acid and alkaline phosphatases. With respect to the activity of urease, the herbicides produced variable effects. The strongest inhibitory effect on the activity of urease was produced by Fuego 500 SC, which reduced the activity of this enzyme by 13.39% when added to soil in a dose exceeding by 160-fold the recommended rate. The RS of the enzymes to the herbicides ranged from 0.461 to 0.955. Urease was the most tolerant to soil contamination with the herbicides.

Effects of Kanwa on Rat Gastrointestinal Phosphatases

2010 ◽  
Vol 3 (3) ◽  
pp. 1147-1152
Author(s):  
Jacob Bamaiyi ◽  
Omajali ◽  
Sanni Momoh
Keyword(s):  
Alkaline Phosphatase ◽  
Small Intestine ◽  
Acid Phosphatase ◽  
Sodium Carbonate ◽  
Elevated Level ◽  
Food Additive ◽  
Alkaline Phosphatases ◽  
Acid And Alkaline Phosphatases ◽  
Diagnostic Indices ◽  
High Level

This study investigates the effects of kanwa on rat gastrointestinal phosphatases. The rats were administered 7% w/v concentration of  trona (Kanwa) orally for a period of two weeks in order to investigate how this compound is being used as food additive in some homes in Nigeria. The Kanwa used in this study was the handpicked variety obtained from sellers from Anyigba market in eastern part of Kogi State, Nigeria. Kanwa, a hydrated sodium carbonate (Na2CO3NaHCO3.2H2O) was obtained as a dried lake salt. Acid phosphatase has the ability to dephosphorylate molecules containing phosphate group. The decreased and elevated level in serum or plasma acid and alkaline phosphatases serves as diagnostic indices for various diseases. Results showed that there was increase and decrease of acid phosphatase (ACP) activities in both the stomach and small intestine. The activities of alkaline phosphatase (ALP) fluctuated in the small intestine. However, in the stomach, an increase activity of ALP was noticed throughout the period of ‘Kanwa’ administration. We concluded that although the level of ‘Kanwa’ consumed in most homes may not be toxic if not taken continuously or repeatedly. Thus, continuous consumption should be discouraged as accumulation of high level of ‘Kanwa’ may cause damages or injuries to the various organs/tissues and may disrupt normal body function.

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.

Biochemical and histochemical studies of alkaline and acid phosphatases in a digenetic trematode,Pegosomum egretti

1986 ◽  
Vol 60 (4) ◽  
pp. 293-298 ◽  
Author(s):  
Indra Rajvanshi ◽  
K. L. Mali
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Raw Materials ◽  
Digenetic Trematode ◽  
Acid Phosphatases ◽  
Alkaline Phosphatases ◽  
Optimum Ph ◽  
Standard Techniques ◽  
Alkaline And Acid Phosphatases

ABSTRACTThe biochemistry and histochemistry ofPegosomum egrettihave been studied using standard techniques. Phosphatases were analysed colorimetrically; the optimum pH for acid phosphatase activity was 5·0 and for alkaline phosphatase was 10·0. The results were compared with those of other trematodes. Histochemical localization of acid and alkaline phosphatases revealed differences in enzyme activity in various tissues. These differences in the site and pattern of distribution of the two enzymes have been discussed in relation to transport of raw materials and the metabolism of the cell concerned.

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.

CYCLIC CHANGES IN THE ACTIVITIES OF PLASMA ACID AND ALKALINE PHOSPHATASES DURING EGGSHELL CALCIFICATION IN THE DOMESTIC FOWL

1965 ◽  
Vol 43 (4) ◽  
pp. 451-457 ◽  
Author(s):  
T. G. Taylor ◽  
Ann Williams ◽  
Jean Kirkley
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Domestic Fowl ◽  
Shell Formation ◽  
Medullary Bone ◽  
Alkaline Phosphatases ◽  
Acid And Alkaline Phosphatases ◽  
Osteoblast Activity ◽  
Main Period ◽  
Cyclic Changes

Acid and alkaline phosphatases were assayed in 240 samples of plasma taken from laying hens at various stages of the laying cycle. The activity of both enzymes was minimal shortly after oviposition. Acid phosphatase values increased rapidly during the first 10 hours of shell formation and then more slowly, reaching a peak when shell calcification was completed. A precipitous fall occurred about the time of oviposition. The activity of alkaline phosphatase increased rapidly after oviposition, reaching a maximum 8–9 hours later when calcification of the next egg had been in progress 4–5 hours, and thereafter falling steadily throughout the main period of shell formation. No systematic changes were observed in the levels of either enzyme at successive bleedings when shell calcification was not in progress. Striking relations were observed between the cyclic changes in the levels of phosphatase activity in the plasma and the changes known to occur in the cell population of the medullary bone, the level of acid phosphatase paralleling the osteoclast activity and the alkaline phosphatase paralleling the osteoblast activity. It is suggested that the osteoclasts and osteoblasts release their respective phosphatase during their active metabolic phases.

Studies on phosphatase systems in hepatopancreatic cells of the molluscan host of Echinoparyphium sp. and in the rediae and cercariae of this trematode

Parasitology ◽  
1964 ◽  
Vol 54 (1) ◽  
pp. 73-79 ◽  
Author(s):  
Thomas C. Cheng
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Technical Assistance ◽  
Public Health Service ◽  
National Institutes Of Health ◽  
University Of Virginia ◽  
Alkaline Phosphatases ◽  
Acid And Alkaline Phosphatases ◽  
School Of Medicine ◽  
The University

1. The distribution of acid and alkaline phosphatases in the hepatopancreatic cells of the molluscan host of Echinoparyphium sp. and in the redia and cercaria of this trematode has been studied.2. There is a heavier concentration of acid phosphatase in the hepatopancreas of infected snails than in uninfected snails.3. No acid phosphatase is present in the bodies of the rediae or cercariae but this enzyme is present in the contents of the redial caeca.4. Alkaline phosphatase activity is greater in the hepatopancreas of infected snails than in uninfected snails.5. Alkaline phosphatase is present in the tissues of the rediae and the cercariae, especially in the fully developed cercariae.6. It is suspected that the increase in acid and alkaline phosphatases in Helisoma trivolvis infected with Echinoparyphium redia is correlated with the breakdown of glycogen by the parasite.This research was made possible by Grants E-3443, E-3443C1, and AI 3443–03 from the Institute of Allergy and Infectious Diseases, National Institutes of Health, U.S. Public Health Service. The author is grateful to Mr Randall W. Snyder, Jr., School of Medicine, The University of Virginia, for technical assistance.

scholarly journals The effect of carfentrazone-ethyl on soil microorganisms and soil enzymes activity / Wpływ karfentrazonu etylu na mikroorganizmy i aktywność enzymów glebowych

2015 ◽  
Vol 41 (3) ◽  
pp. 3-10 ◽  
Author(s):  
Monika Tomkiel ◽  
Małgorzata Baćmaga ◽  
Jadwiga Wyszkowska ◽  
Jan Kucharski ◽  
Agata Borowik
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Soil Microorganisms ◽  
Soil Microbial Communities ◽  
Optimal Dose ◽  
Colony Development ◽  
Soil Microbial ◽  
Oligotrophic Bacteria ◽  
Organotrophic Bacteria ◽  
Soil Enzymes Activity

Abstract The aim of this study was to determine the effect of carfentrazone-ethyl (CE) doses of 0.265, 5.280, 10.560, 21.180, 42.240 μg kg-1 soil DM on fungi, Acnomycetes, organotrophic bacteria, total oligotrophic bacteria and spore-forming oligotrophic bacteria, and on the activity of dehydrogenases, catalase, urease, alkaline phosphatase, acid phosphatase, arylsulfatase and β-glucosidase. Carfentrazone-ethyl had a stimulating effect on total oligotrophic bacteria and organotrophic bacteria, but it inhibited the growth of Azotobacter, fungi, spore-forming oligotrophic bacteria and Actinomycetes. The analyzed substance modified the structure of soil microbial communities, and it induced the most profound changes in fungi. The highest values of the colony development (CD) index and the eco-physiological (EP) index were observed in organotrophic bacteria. The optimal dose of carfentrazone-ethyl stimulated the activity of dehydrogenases, catalase, urease, alkaline phosphatase, acid phosphatase and β-glucosidase, but it had no effect on arylsulfatase. The highest doses of the analyzed substance inhibited the activity of dehydrogenases (reduction from 11.835 to 11.381 μmol TPF), urease (reduction from 0.545 to 0.500 mmol N-NH4) and arylosulfatase (reduction from 0.210 to 0.168 mmol PNP). Dehydrogenases were most resistant to CE, whereas acid phosphatase and arylsulfatase were least resistant to the analyzed compound

Ultracytochemical Localization of Aryl Sulfatase, Esterase, and Acid and Alkaline Phosphatases with 4-Nitrocatechol Substrates and Tetrazolium Salts

1974 ◽  
Vol 32 ◽  
pp. 226-227
Author(s):  
W. Allen Shannon ◽  
Yoshinobu Hoshino ◽  
Hannah L. Wasserkrug ◽  
Arnold M. Seligman
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Adrenal Cortex ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Alkaline Phosphatases ◽  
Cytochemical Localization ◽  
Rat Kidney Cortex ◽  
Aryl Sulfatase ◽  
Tetrazolium Salts

The ultra cytochemical localization of various hydrolases, i. e, aryl sulfatase(ArS), esterase (Est), acid phosphatase(AcP) and alkaline phosphatase (A1P) is demonstrated in rat kidney cortex with newly developed 4-nitrocatechol substrates (2-hydroxy-5-nitrophenyl compounds) (Fig. 1) and tetrazolium salts, Nitro-BT, BSPT, and BPPT. ArS was also investigated in adrenal cortex.

Effect of Alkaline and Acid Phosphatases on Clotting:

1966 ◽  
Vol 15 (03/04) ◽  
pp. 365-380 ◽  
Author(s):  
P. G Iatridis ◽  
J. H Ferguson
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Inhibitory Effect ◽  
Factor Ix ◽  
Acid Phosphatases ◽  
Acid And Alkaline Phosphatase ◽  
Direct Inhibitory Effect ◽  
Alkaline And Acid Phosphatases

SummaryAlkaline phosphatase is found to enhance the activation of factor IX by SF. The correlation of the distribution of alkaline phosphatase in electrophoretic fractions with the clotting tests suggest that the “beta” fraction contains the responsible factor for the acceleratory effect of alkaline phosphatase on clotting.Acid phosphatase, while not exerting a direct inhibitory effect on SF, does enhance the plasmatic anti-SF activity. The “beta” and “F-gamma” fractions seem to contain the responsible factor of acid phosphatase for the plasmatic anti-SF enhancement.SF preparation has no acid or alkaline phosphatase activity.A tentative schema is proposed to explain the effects of acid and alkaline phosphatase on clotting.

Studies on phosphatase systems of cestodes I. Studies on Taenia pisiformis (Cysticercus and adult)

Parasitology ◽  
1957 ◽  
Vol 47 (1-2) ◽  
pp. 70-80 ◽  
Author(s):  
David A. Erasmus
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Life Cycle ◽  
Acid Phosphatase ◽  
Active Transport ◽  
Relative Magnitude ◽  
Alkaline Phosphatases ◽  
Biochemical Tests ◽  
Acid And Alkaline Phosphatase ◽  
Histochemical Tests

1. The phosphatases present in the adult and cysticercus stages of Taenia pisiformis have been investigated using histochemical and biochemical methods.2. Histochemical tests failed to demonstrate the sites of enzyme activity in the cysticercus.3. In the adult, the acid phosphatase is confined to the cuticle. Alkaline phosphatase occurs in the cuticle, subcuticular cells and the membranes bounding the ovary and vitelline tubules.4. The histochemical distribution is uneven along the length of the worm, both acid and alkaline phosphatase being predominant hi the region of ‘mature’ proglottides. The scolex was negative to both tests.5. Biochemical tests have demonstrated distinct acid and alkaline phosphatases in the cysticercus and adult stages. In the cysticercus the acid enzyme is predominant and in the adult it is the alkaline, implying a change in relative magnitude during the completion of the life cycle.6. pH-activity curves have been obtained for the enzymes of both stages.7. The results are discussed in relation to recent findings in the field of cestode enzymology, and it is suggested that these phosphatases may be associated with active transport of materials across the cuticle and ovarian and vitelline membranes.

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