scholarly journals Effect of heating oil on the activity of soil enzymes and the yield of yellow lupine

2011 ◽  
Vol 52 (No. 5) ◽  
pp. 220-226 ◽  
Author(s):  
J. Kucharski ◽  
E. Jastrzębska
Keyword(s):  
Alkaline Phosphatase ◽  
Soil Enzymes ◽  
Urease Activity ◽  
Alkaline Phosphatases ◽  
Acid And Alkaline Phosphatases ◽  
Heating Oil ◽  
Average Activity ◽  
Yellow Lupine ◽  
Experimental Soil ◽  
Limed Soil

The aim of the study was to determine the response of soil enzymes such as dehydrogenases, urease and acid and alkaline phosphatases to heating oil contaminating (0.0, 0.25, 0.5, 0.75, 1.0, 1.5% of soil) the experimental soil supplemented with lime and used for cultivation of yellow lupine of the Markiz variety. An increasing contamination of soil with heating oil stimulated the activity of dehydrogenases and acid and alkaline phosphatases but had a toxic effect on yellow lupine. Lime supplements did not have a significant effect on an average activity of soil dehydrogenases. However, such soil treatment had a significant effect on urease. Increasing heating oil doses in lime-supplemented soil stimulated urease activity, whereas in lime-free soil urease activity was inhibited. The activity of acid and alkaline phosphatase was lower in limed soil than in lime-free soil. The activity of dehydrogenases, urease and alkaline phosphatase in the soil with lupine cultivation was significantly higher than in the unsown soil.

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.

Histochemical and electrophoretic studies on phosphatases of some Indian trematodes

1982 ◽  
Vol 56 (2) ◽  
pp. 111-116 ◽  
Author(s):  
Masoodul Haque ◽  
Ather H. Siddiqi
Keyword(s):  
Alkaline Phosphatase ◽  
Gel Electrophoresis ◽  
Water Buffalo ◽  
Polyacrylamide Gel Electrophoresis ◽  
Bubalus Bubalis ◽  
Alkaline Phosphatases ◽  
Acid And Alkaline Phosphatases ◽  
Gastrothylax Crumenifer ◽  
Acid And Alkaline Phosphatase ◽  
Fasciolopsis Buski

ABSTRACTThe isoenzymes of acid and alkaline phosphatases and their histochemical localization were studied by polyacrylamide disc gel electrophoresis in four species of trematodes: Gigantocotyle explanatum from the liver and Gastrothylax crumenifer from the rumen of water buffalo (Bubalus bubalis) and Echinostoma malayanum and Fasciolopsis buski from the small intestine of the pig (Sus scrofa). Both acid and alkaline phosphatases were present in the tegument, gastrodermis, suckers, testes, ovary, eggs, vitellaria and uterus but alkaline phosphatase activity was demonstrated only in the parenchyma and excretory ducts. Polyacrylamide gel electrophoresis revealed two to four isoenzymes for both acid and alkaline phosphatase.

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.

Progestation

1967 ◽  
Vol 56 (3_Suppla) ◽  
pp. S7-S45 ◽  
Keyword(s):  
Tritiated Thymidine ◽  
Succinic Dehydrogenase ◽  
Glandular Epithelium ◽  
Synthetic Activity ◽  
Cell Renewal ◽  
Pulse Labelling ◽  
Uterine Receptivity ◽  
Alkaline Phosphatases ◽  
Monocytic Cells ◽  
Acid And Alkaline Phosphatases

ABSTRACT Autoradiographic, enzymic and histologic studies on uteri of pregnant rats were carried out to follow the endometrial modifications which take place during progestation (days L0 – L4) and culminate in the state of uterine receptivity essential for ovum-implantation. Pulse labelling with tritiated thymidine (radioactive DNA precursor) on L0, L1 and L2 revealed a sequence of cell renewal in luminal and glandular epithelium and endometrial stroma. On L3 and L4 stromal cells showed extensive incorporation of tritiated thymidine. This synthetic activity was associated with endometrial preparation for decidualization and was evoked at least in part, by the surge of oestrogen on L3. All layers of the uterine wall were heavily infiltrated on L0 and resembled the site of an acute inflammatory reaction. Subsequently, polymorphonuclear infiltration diminished and monocytic cells predominated. On L3 a spatial arrangement was observed: eosinophiles were concentrated in the basal endometrium and monocytic cells in the subepithelial stroma. A comparison was made between such a shift in migratory cells in the uterus and similar phenomena which occur in inflammatory and immune reactions. Activities of acid and alkaline phosphatases, of ATP-ase and succinic dehydrogenase were low on L0 and L1 during the periods of infiltration, degeneration and regeneration of luminal and glandular epithelium. Enzymic activities increased on the following days, (L3 and L4). Vascular dilation and engorgement and endometrial oedema were observed near the blastocysts on L4. Most blastocysts incorporated tritiated thymidine after 14.00 h on L4, but some showed uptake before loss of the zona which occurs usually between 14.00 and 16.00 h; therefore, it was assumed that the permeability of the zona increases prior to being shed. Activities of succinic dehydrogenase and acid and alkaline phosphatases were demonstrable in blastocysts on L4 while they were still »free« in the uterine lumen.

Soil response to chemicals used in a field experiment

2013 ◽  
Vol 27 (2) ◽  
pp. 151-158 ◽  
Author(s):  
S. Jezierska-Tys ◽  
A. Rutkowska
Keyword(s):  
Alkaline Phosphatase ◽  
Enzymatic Activity ◽  
Field Experiment ◽  
Soil Microorganisms ◽  
Block Design ◽  
Soil Samples ◽  
Alkaline Phosphatases ◽  
Soil Response ◽  
Negative Effect ◽  
Set Up

Abstract The effect of chemicals (Reglone 200 SL and Elastiq 550 EC) on soil microorganisms and their enzymatic activity was estimated. The study was conducted in a field experiment which was set up in the split-block design and comprised three treatments. Soil samples were taken six times, twice in each year of study. The results showed that the application of chemicals generally had no negative effect on the number of soil microorganisms. The application of Reglone 200 SL caused an increase of proteolytic and ureolytic activity and affected the activity of dehydrogenases, acid and alkaline phosphatases in the soil. The soil subjected of Elastiq 550 EC was characterized by lower activity of dehydrogenases, protease, urease and alkaline phosphatase.

Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified isoenzymes from humans.

1976 ◽  
Vol 22 (7) ◽  
pp. 972-976 ◽  
Author(s):  
H Van Belle
Keyword(s):  
Alkaline Phosphatase ◽  
Substrate Concentration ◽  
Human Liver ◽  
Alkaline Phosphatases ◽  
Mechanism Of Inhibition ◽  
Optimum Ph ◽  
Alkaline Phosphatase Isoenzymes

Abstract I studied the kinetics and sensitivity toward inhibition by levamisole and R 8231 of the most important human alkaline phosphatase isoenzymes. N-Ethylaminoethanol proved superior to the now widely used diethanolamine buffer, especially for the enzymes from the intestine and placenta, behaving as an uncompetitive activator. The optimum pH largely depends on the substrate concentration. The addition of Mg2+ has no effect on the activities. The meaning of Km-values for alkaline phosphatases is questioned. Isoenzymes from human liver, bone, kidney, and spleen are strongly inhibited by levamisole or R 8231 at concentrations that barely affect the enzymes from intestine or placenta. The inhibition is stereospecific, uncompetitive, and not changed by Mg2+. Inhibition is counteracted by increasing concentrations of N-ethylaminoethanol. The mechanism of inhibition is suggested to be formation of a complex with the phosphoenzyme.

An Immunoprecipitation Assay for High Molecular Weight Alkaline Phosphatase in Human Serum

1989 ◽  
Vol 26 (2) ◽  
pp. 151-157 ◽  
Author(s):  
Gerald A Maguire ◽  
Halima Adnan
Keyword(s):  
Molecular Weight ◽  
Alkaline Phosphatase ◽  
Liver Disease ◽  
High Molecular Weight ◽  
Solid Phase ◽  
Bone Alkaline Phosphatase ◽  
Intestinal Alkaline Phosphatase ◽  
Alkaline Phosphatases ◽  
Molecular Weight Form ◽  
Hepatic Malignancies

The serum of patients with obstructive liver disease may contain a high molecular weight form of alkaline phosphatase (high Mr alkaline phosphatase). The presence of this form of alkaline phosphatase is associated with hepatic malignancies. We have investigated the use of anti-alkaline phosphatase monoclonal antibodies which do not bind high Mr alkaline phosphatase in assays for high Mr alkaline phosphatase. Direct immunoprecipitation of liver and bone alkaline phosphatase with solid phase anti-liver alkaline phosphatase antibody (which also reacts with bone alkaline phosphatase) and measurement of the residual supernatant alkaline phosphatase activity led to a precise assay. Intestinal alkaline phosphatase interfered in this assay which, consequently, was of little use in the differential diagnosis of liver disease. Indirect precipitation of liver, bone, placental and intestinal alkaline phosphatase by soluble anti-liver alkaline phosphatase (which reacts with liver and bone alkaline phosphatases), soluble anti-intestinal alkaline phosphatase (which reacts with placental and intestinal alkaline phosphatases) and solid phase anti-mouse IgG led to an assay which, although less precise, showed more promise of being useful clinically.

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