• The Korean Journal of Pharmacology
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• v.9 no.1
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• pp.47-51
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• 1973

A benzomorphan derivative, pentazocine has both opioid agonistic actions and weak narcotic antagonistic activity. In this paper, authors attempted to study the dose response of pentazocine on the blood sugar level, serum transaminase and alkaline phosphatase activity in rabbits. Eighteen rabbits were devided into 3 groups, and each group were injected with pentazocine 5mg, 15mg, and 30mg/kg respectively. And metabolic effects were investigated measuring the change of blood sugar contents, serum transaminase (S-GOT, S-GPT) activities and alkaline phosphatase activities in rabbits. The results were obtained as follows; 1. Pentazocine significantly increased the blood sugar content in rabbits. 2. Pentazocine significantly increased the serum GOT activity but in the serum GPT activity, it significantly increased in large dose. 3. Pentazocine significantly increased serum alkaline phosphatase activity.

• BMB Reports
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• v.32 no.3
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• pp.294-298
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• 1999

Myo-inositol monophosphate phosphatase is a key enzyme in the phosphoinositide cell-signaling system. Incubation of myo-inositol monophosphate phosphatase from porcine brain with N-bromosuccinimide (NBS) resulted in a time-dependent loss of enzyme activity. The inactivation followed pseudo-first-order kinetics with the second-order rate constant of $3.8{\times}10^3\;M^{-1}min^{-1}$. The time course of the reaction was significantly affected by the substrate myo-inositol-1-phosphate, which afforded complete protection against the loss of catalytic activity. Spectrophotometric studies indicated that about one oxindole group per molecule of enzyme was formed following complete loss of enzymatic activity. It is suggested that the catalytic function of myo-inositol monophosphate phosphatase is modulated by the binding of NBS to a specific tryptophan residue at or near the substrate binding site of the enzyme.

• Korean Journal of Microbiology
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• v.23 no.2
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• pp.90-100
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• 1985

The present study was designed to investigate cellular regulation of phosphate metabolism between catabolically repressed and derepressed states in yeast (Saccharomyces uvarum). The activities of various phospatases and the contents of phosphate compounds were detected according to the culture phase and various phosphate concentrations. As the results, Saccharomyces uvarum derepressed many phosphate metabolizing enzymes such as alkaline phosphatase, acid phosphatase and ATPase more than ten fold simultaneously during catabolic repression (phospgate and sugar starvation). At the same state, the amounts of orthophosphate, nucleotidic labile phosphate and acid soluble polypgosphate were increased, compared to basal levels of normally cultivated cells. $Mg^{++}-stimulated$ type among all phospatases was appeared to have most of the enzyme activity. It could be postulated that $K^+ -stimulated$ alkaline phosphatase was directly or indirectly correlated with the synthesis of acid insoluble polyphosphate $Mg^{++}-stimulated$ phosphatase with the degradation of polyphosphates. In case of cultivation in the medium supplemented with sugar and phosphate (catabolic derepression), phospgatase activities except for alkaline phosphatase were decreased rapidly through the progressive batch culture, After 12 hrs culture, at early exponential phase, the cellular accumulation of acid insoluble polyphosphate increased about 5 fold, compared to those of the starved cells. Under catabolic repression, it could be postulated that intracellular phosphate metabolism was regulated by derepressions of phosphatases. The function of polyphosphate system was shown to compensate the ATP/ADP system as phosphate donor and energy source especially during catabolic repression.

• Korean Journal of Environmental Biology
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• v.17 no.4
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• pp.493-498
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• 1999

To verify the usefulness of enzyme activities as a index for the stability or maturity of organic refuse composting such as grape pomace, Vmax of $\beta$-glucosidase, cellobiohydrolase and alkaline phosphatase were measured. The peak values of all measured enzymes at the initial stage of composting were probably associated with easily degradable organic matter in the grape pomace and decreased gradually. But the activities of $\beta$-glucosidase and cellobiohydrolase were increased again rapidly whereas that of alkaline phosphatase remained approximately constant after 60 composting days. These results suggest that the increase of enzyme activities during the later periods of grape pomace composting process could be used as a index for their stability.

• 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.

• Journal of Microbiology and Biotechnology
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• v.13 no.5
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• pp.660-665
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• 2003

High-level expression of Thermus caldophilus GK24 alkaline phosphatase (Tca APase) was achieved in Escherichia coli using the pET-based expression plasmids, pEAP1 and pEAP2. In the case of plasmid pEAP2, the signal peptide region of Tca APase was replaced by the PelB leader peptide of expression vector pET-22b(+). Furthermore, the expression level was somewhat higher than that of plasmid pEAPl. A rapid purification procedure of Tca APase overproduced in E. coli was developed which involved heating to denature E. coli proteins followed by HiTrap Heparin HP column chromatography. Optimal temperature and pH and $Mg^{2+}$ dependence of the recombinant Tca APase were similar to those of native enzyme isolated from T. caldophilus GK24.

• BMB Reports
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• v.30 no.4
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• pp.262-268
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• 1997

The thermophilic and thermostable alkaline phosphatase was purified to near homogeneity from the osmotic lysis of Thermus caldophilus GK24, The purified enzyme had an apparent molecular mass of 108, 000 Da and consisted of two subunits of 54,000 Da. lsoelectric-focusing analysis of the purified enzyme showed a pi of 7.3. The enzyme contained two Cys residues, and its amino acids composition was quite different from that of Thermus aquaticus YT-1 alkaline phosphatase and Escherichia coli alkaline phosphatase, The optimum pH and temperature of the enzyme were 11.0-11.5 and $80^{\circ}C$ respectively. The enzyme was stable in the pH range of 9.0-12.0 at $25^{\circ}C$ for 36 h. and the half-life at $80^{\circ}C$ (pH 11.0) was 6 h. The enzyme was activated by $MgCl_2$ and inhibited by EDTA. With ${\rho}-nitrophenyl\;phosphate\;({\rho}NPP)$ as the substrate, the enzyme had a Michaelis constant $(K_m) $of $3.6{\times}10^{-5}M$, The enzyme preferentially hydrolyzed the phosphomonoester bond of AMP in ribonucleotides and glycerophosphate.

• Korean journal of applied entomology
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• v.34 no.2
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• pp.95-99
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• 1995

Acid phosphatase(AP) of he aphid, Megoura crassicauda and the major component of the lady beetle's artificial diet, fresh chicken liver, was adapted as a model protein to study the digestion of diet proteins in the midgut of Harmonia axyridis. The lady beetle did not secrete its own AP into the lumen of the midgut. The aphid and the live chicken liver had AP which was still alive in enzymatic activity from the extract of the lumen of the midgut of the lady beetle. The digestive ability of the lady beetle on proteins turned out to be different depending on food sources. In the lumen of the midgut of the lady beetle, though most of AP of live chicken liver lost its activity withtin 12 hours, that of M. cassicauda kept strong enzymatic activity up to 24 hours.

• BMB Reports
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• v.29 no.5
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• pp.417-422
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• 1996

In clonal sublines with different metastatic ability derived from Dunning rat prostate tumor, phosphoamino acid levels of cellular proteins were determined. Cell lines with high metastatic ability exhibited 5-fold higher phosphotyrosine level than did cell lines with low metastatic ability, while the contents of phosphoserine and phosphothreonine were similar among cell lines examined, All cell lines showed similar activities of protein tyrosine kinases as well as overall protein kinases. Phosphotyrosine protein phosphatase (PTPP) activities of the cells with high metastatic ability were very low, compared to those of the cells with low metastatic ability, suggesting that the different phosphotyrosine levels among the cell lines were due to the difference in PTPP activities rather than protein tyrosine kinase activities. Cellular activities of prostatic acid phosphatase (PAcP), which has been reported to possess phosphotyrosine protein phosphatase activity, were shown to be inversely related to the phosphotyrosine levels and metastatic abilities of the prostate tumor cells, These results suggest that cellular PAcP activity, regulating phosphotyrosine levels of cellular proteins, is closely connected with the metastatic process in prostate tumor cells and can be utilized as a good biochemical marker for the diagnosis of metastasis of prostate tumor.

• The Korean Journal of Ecology
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• v.14 no.1
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• pp.101-111
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• 1991

Amoeba sp. was cultured under the light and the dark conditions, and the activity of phosphatases was investigated. There was a linear correlation between the early reaction time and the activity of phosphatases when phosphatases were incubated at 30℃. Then the activity of acid phosphatase was about 2 times higher than that of alkaline phosphatase. The activity of phosphatase was optimal at pH 5.0 in acidic part and at pH 8.0 in alkaline part, respectively. The optimal temperature of phosphatases was near the 40℃. The isozyme patterns of cytoplasmic acid phosphatase were compared with those of membraneous one. Both the isozyme patterns were shown to bo polymorphic on the polyacyamide gel, but different band patterns were observed in the isozymes of the cytoplasmic and the membraneous acid phosphatases. The number of Amoeba sp. under the light stimulus for 48 hours decreased negative exponentially from the illumination. The activity of acid and alkaline phosphatases under the illumination of light incresed 1.7 and 1.5 times higher, respectively, than the activity of those under the dark condition. This result apperars to be related to the mechanism of the autophosphorylation.