Effects of Kanwa on Rat Gastrointestinal Phosphatases

Author(s):  
Jacob Bamaiyi ◽  
Omajali ◽  
Sanni Momoh

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.

1965 ◽  
Vol 43 (4) ◽  
pp. 451-457 ◽  
Author(s):  
T. G. Taylor ◽  
Ann Williams ◽  
Jean Kirkley

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.


Parasitology ◽  
1964 ◽  
Vol 54 (1) ◽  
pp. 73-79 ◽  
Author(s):  
Thomas C. Cheng

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.


2011 ◽  
Vol 52 (No. 5) ◽  
pp. 220-226 ◽  
Author(s):  
J. Kucharski ◽  
E. Jastrzębska

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.


Author(s):  
Ragnar Fänge

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.


1982 ◽  
Vol 56 (2) ◽  
pp. 111-116 ◽  
Author(s):  
Masoodul Haque ◽  
Ather H. Siddiqi

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.


1986 ◽  
Vol 60 (4) ◽  
pp. 293-298 ◽  
Author(s):  
Indra Rajvanshi ◽  
K. L. Mali

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.


1967 ◽  
Vol 15 (6) ◽  
pp. 311-334 ◽  
Author(s):  
B. K. WETZEL ◽  
S. S. SPICER ◽  
R. G. HORN

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.


Biologia ◽  
2008 ◽  
Vol 63 (6) ◽  
Author(s):  
Christina Hadjivanova ◽  
Nikolina Tzvetkova

AbstractThe activities of acid and alkaline phosphatases along with phosphorus content in leaves of European beech (Fagus sylvatica L.) were studied for a period from April to October. The phosphorus content of beech leaves was highest in April, at the beginning of the vegetation period; from May to October it was twofold lower than in April. Acid phosphatase activity (per unit fresh weight) in leaves collected from the middle part of the crown decreased significantly in May and July compared to the enzyme activity in April. In both the low and middle parts of the crown, the acid phosphatase activity had a peak in August, and thereafter decreased in September and October. No correlations between acid phosphatase activity and phosphorus concentrations were found. Alkaline phosphatase activity was very low and in some cases near the detection limit during the whole observation period.


1972 ◽  
Vol 27 (8) ◽  
pp. 973-976
Author(s):  
Shakila Aziz ◽  
S. N. Hasnain ◽  
M. Zain-Ul-Abedin

1. Acid phosphatase (AcPase) and alkaline phosphatase (AlPase) activities and specific activities were determined in six different tissues of Uromastix during active and hibernating periods.2. The protein concentration was significantly reduced in all the tissues during hibernation.3. pH optima of acid and alkaline Pases were found to be 4.2 and 9.2 respectively.4. AcPase activity was increased in all the tissues except liver and small intestine during hibernation.5. AlPase activity was increased in all the tissues except small intestine during hibernation.6. Specific activities of both the enzymes were increased during hibernation.


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