• The Korean Journal of Food And Nutrition
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• v.8 no.1
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• pp.1-5
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• 1995

ATPase was the most available phosphatase in culture broth of 5. coli P90C. To measure the stable phosphatase activity it was necessary to react nth reaction reagent over 30 min and then we can get stable optical density at 410 m. Transfer time from preculture to main culture for the production of $\beta$-glactosidase was good after 3 hrs cultivation. Phosphatase activity was highest at log phase in main culture and as the cell begins to make $\beta$-galactosidase phosphatase activity begins to decrease.

• The korean journal of orthodontics
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• v.26 no.4
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• pp.449-454
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• 1996

The propose of this study was to evaluate the difference of cellular activity dependent on intermittent compressive force by determining the alkaline phosphatase activity. Alkaline phosphatase activity was measured on control and experimental groups every 24, 48, 72hours. Experimental groups consisted of continous and intermittent compressive group which were compressed by $300gm/cm^2$ of diaphram pump. The intermittent compressive group was connected by timer which was worked on 10 minutes an off 10 minutes. The results were as follows; 1. The alkaline phosphatase activity between control and experimental groups showed not significant difference at compressed 24 hours. 2. The alkaline phosphatase activity of experimental groups were more increased than control group at compressed 48 hours. 3. The alkaline phosphatase activity of intermittent compressive group showed significant increased to control group. Whereby continuous compressive group showed not significant difference to control at 72 hours. 4. The alkaline phosphatase activity of intermittent compressive group were stringly increased than continuous compressive groups. 5. Between experimental groups and control group no other morphologic changes were detected by microscopic findings.

• Biomedical Science Letters
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• v.5 no.1
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• pp.119-129
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• 1999

This study was aimed to investigate the enzyme-histochemical localization and characteristics of alkaline and acid phosphatase extracted from adult of Echinostoma hortense. Using the Gomori calcium stain and the Gomori lead nitrate satin method, we found that the alkaline and acid phosphatases were localized mostly in the intestine, vitellaria and pharynx of Echinostoma hortense. The three isozymes of alkaline phosphatase and two isozymes of acid phosphatase were separated from Echinostoma hortense by electrophoresis. The isozymes of alkaline phosphatase were 145.9, 207.5, 220.8 kDa and the isozymes of acid phosphatase were 179.5 and 209.4 kDa. The activity of alkaline phosphatase was denatured completely after heating at 9$0^{\circ}C$ for 12 seconds. The optimum pH and temperature for activity of alkaline phosphatase were about pH 9 and 4$0^{\circ}C$, while the optimum pH for activity of acid phosphatase was about pH 5. The maximum activity of alkaline phosphatase was at 189 unit, but maximum activity of acid phosphatase was at 71 unit As the result from above, we observed that alkaline and acid phosphatases funtion mainly in the alimentary tract and vitellaria. Echinostoma hortense performs the parasitism in the intestine of host by using proper isozyme of phosphatase.

• Journal of Life Science
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• v.21 no.1
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• pp.31-35
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• 2011

Dual-specificity protein phosphatases (DUSPs) constitute a family of protein phosphatase characterized by the ability to dephosphorylate phospho-tyrosyl and phospho-seryl/threonyl residues. Most DUSPs are involved in regulation of cell survival and differentiation. In this study, a human dual-specificity protein phosphatase, DUSP28, was isolated from a human kidney cDNA. The recombinant protein was successfully produed in E.coli and showed sufficient phosphatase activity toward DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate). Various phosphatase inhibitors and divalent metals were tested for their effects on the DUSP28 phosphatase activity. As a result, $Zn^{2+}$ was found to strongly inhibit DUSP28 phosphatase activity, suggesting DUSP28 is involved in Zn-related signal transduction pathway. Furthermore, the DUSP28 protein preferred phospho-tyrosyl residues to phospho-threonyl residues, implying its physiological roles in the cellular process.

• The Korean Journal of Zoology
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• v.36 no.3
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• pp.425-432
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• 1993

Alkaline phosphatase from Culex pipiens pallens was examined to determine the optimal assay condition and to assay the activity during ovarian development. The activity of alkaline phosphatase in a male and a nongravid female continuously were declined after eclosion. But by the stimulus of a blood meal, the enzyme activity was increased dramatically. At 30 hr. after a blood meal, the maximal activity was reached and then declined. And after 48 hr. after a blood meal, the second activity increase was revealed. This second increase was maintained up to oviposition. The first activity increase was revealed in the midgut and the second increase was done in the ovary to assay the organ distribution of alkaline phosphatase. In electrophresis data, it was shown 5 isozyme bands, ALP-1 and ALP-2 in the ovary, ALP-3 in the thorax and the midgut, and ALP-4 and ALP-5 in the thorax, the fatbody and the midgut in crude extract at 30 hr. after a blood meal. One the same ovary pattern were shown at 72 hr. after a blood meal.

• Asian-Australasian Journal of Animal Sciences
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• v.2 no.2
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• pp.99-102
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• 1989

The level of serum alkaline phosphatase activity was determined in 7 Japanese Black steers at different ages. The isoenzyme activity of non-bone origin was estimated using a heat-inactivation technique. The activity of serum alkaline phosphatase (SALP, K-A unit) decreased as age (AGE, mo.) increased: SALP = 14.15 - 0.17 (${\pm}\;0.03$) AGE, r = -0.81, P<0.01, $S.E.\;{\pm}\;0.28$. The variation of the activity was greater in younger age than the older. The temperature of $58^{\circ}C$ for the treatment of heat inactivation of bovine serum appeared to be suitable. The percentage of heat inactivated enzyme activity negatively correlated with age and positively with the level of serum alkaline phosphatase activity. The activity of SALP of non-bone origin was inferred to stay at about constant level irrespective of age and that of bone origin decreased with age.

• YAKHAK HOEJI
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• v.36 no.2
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• pp.129-136
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• 1992

The effects of ginseng saponins, gypsophila saponin, sodium dodecyl sulfate(SDS), and Triton X-100 on membrane $K^+-dependent$ phosphatase activity which is lipid dependent and represents dephosphorylation step of the complete Na+, $K^+-ATPase$ reaction were investigated in this study to elucidate whether the effects of ginseng saponins are due to the detergent action, using sarcolemma enriched preparation isolated from dog ventricle. $Na^+$, $K^+-ATPase$ and $K^+-dependent$ phosphatase activities of cardiac sarcolemma were about $143\;{\mu}mol$ Pi/mg protein/hr and $34\;{\mu}mol$ p-nitrophenol/mg protein/hr, respectively. While ginseng saponins (triol>total>diol) inhibited $K^+-dependent$ phosphatase activity, gypsophila saponin, and low dose of SDS($0.4\;{\mu}g/{\mu}g$ protein), and Triton X-100 ($0.6\;{\mu}g/{\mu}g$ protein) increased the enzyme activity, indicating disruptive effect of detergents on membrane barriers. The activating effect of low doses of Triton X-100 on membrane $K^+-dependent$ phosphatase appeared at concentration decreasing light scattering. However, the inhibitory effect of ginseng saponin appeared before a decrease in light scattering. These results suggest that low concentrations of ginseng saponins inhibit the membrane $K^+-dependent$ phosphatase by interacting directly with enzyme before membrane disruption.

• The Korean Journal of Zoology
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• v.23 no.2
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• pp.61-68
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• 1980

Quantitative analysis of the activities of transport ATPases as well as alkaline phosphatase of the mouse uterus was carried out during the estrous cycle. Even though the proportional patterns of the enzyme activities were similar each another between the stages of estrous cycle, the absolute activities of the enzymes except $K^+$-dependent and $Na^+$, $K^+$-activated ATPases at the time of estrus were significantly (p<0.025) higher than that at any other time of the estrous cycle. That is, the activities of $K^+$-dependent and $Na^+$, $K^+$-activated ATPases were negligible during the period of time from diestrus to estrus while the little activities (0.04 $\\sim$ 0.05$\\mu$M/mg protein/hr in average, $6\\sim7$% of the total enzyme activity) of these enzymes appeared at the time of metaestrus. On the other hand, at the time of estrus, the activities of $Mg^++$-dependent phosphatase, transport ATPase and alkaline phosphatase were rapidly and tremendously increased to be 0.69 (35%), 0.42 (21%) and 1.58 (79%), respectively. The activity of alkaline phosphatase was in the range of 0.60 $\\sim$ 1.58 (79 $\\sim$ 90%) and predominant throughout the estrous cycle. The activity of $Mg^++$-dependent alkaline phosphatase was estimated as 12 $\\sim$ 16% of the total enzyme activity. Therefore, it is assumed likely that $K^+$-dependent and $Na^+$, $K^+$-activated ATPases are not the main factors to control the fluid accumulation at the time of estrus, but may be the factors to reabsorb the luminal fluid into the uterine epithelium at the time of metaestrus, and that $Mg^++$-dependent phosphatase, transport ATPase and alkaline phosphatase must be closely involved in the secretion of luminal fluid from the epithelial cells of the mouse uterus.

• Korean Journal of Veterinary Research
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• v.11 no.2
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• pp.141-143
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• 1971

The serum alkaline phosphatase activity was determined with 64 Korean cattles in different sexe and age groups, using p-nitrophenylphosphate as the substrate. The results obtained were as follows: 1. The mean value of serum alkaline phosphatase activity in Korean cattle was $1.78{\pm}0.21$ Bessey-Lowry units/ml, and $1.71{\pm}0.21$ units/ml. in female and $1.86{\pm}0.21$ units/ml. in male, respectively. 2. The serum alkaline phosphatase activity decreased with age from 4 years group. 3. No statistical significance was recognized among the sexes, but difference among the age groups was found to be highly significant.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.43 no.5
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• pp.540-546
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• 2010

We investigated variations in alkaline phosphatase (APase) activity and alkaline phosphatase hydrolyzable phosphorus (APHP) in northern Gamak Bay from September to December 2009. Dissolved inorganic nitrogen (DIN) and dissolved inorganic phosphorus (DIP) decreased gradually, and the DIN/DIP ratio was higher than the Redfield ratio (16) based on molecular concentrations during most of the observation period. The total APase (T-APase) activity increased with decreasing DIP concentration; i.e., the Relationship between T-APase and DIP showed a high negative correlation (r=-0.80, P<0.001), with APase activity being a good indicator of DIP limiting the Redfield ratio. The T-APase was positively correlated with the concentration of chlorophyll a (r=0.73, P<0.001). This suggests that a major portion of APase activity in northen Gamak Bay seawater is attributed to phytoplankton. The proportion of APHP among dissolved organic phosphorus (DOP) was low in September and high in November. Thus, APase-producing phytoplankton may be able to grow by utilizing APHP as a phosphorus source in autumn when DIP is limiting. Thus, APase activity and the use of DOP by phytoplankton may play an important role in the growth of phytoplankton under DIP limiting conditions such as those of northern Gamak Bay.