• Parasites, Hosts and Diseases
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• v.34 no.1
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• pp.69-78
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• 1996

This study was done to investigate the enzyme-histochemical localization and characteristics of alkaline and acid phosphatase related with metabolism in sparganum and adult of Spirometrn erinacei. By the enzyme-histochemical assay, the alkaline and acid phosphatases were localized in the tegument and subtegumental musculature of sparganum and adult, but not in the parenchyma. The activities of alkaline phosphatase were stronger in the tegument than in the subtegumental musculature, and activities of acid phosphatase were stronger in the tegument of adults than those of sparganum. The 2 isozymes of alkaline and acid phosphatases were separated from s-sparganum (from snake) and r-sparganum (from experimentaly infected rats) respectively but 4 isozymes of Alp and 3 isoxymes of Acp were separated from adult worms by electrophoresis. In isogyme Alp, the 661)a was the common isozyme, but 130 kDa isozyme of Acp was the common isozyme in spargana and adult worms. By isoelectrofocusing, 4 isozymes (PI 7.9, 7.7, 6.5 and 6.3) and 2 isozymes (PI 7.9 and 7.7) of alkaline phosphatase were separated from adults and spargana respectively. In the stability against heat, activity of alkaline phosphatase was denatured perfectly after heating at 90℃ for 40 seconds. The optimum pH and temperature for activity of alkaline phosphatase were about pH 10 and 50℃, respectively. The maximum activity (unit) of alkaline phosphatase was 22.0 in s- sparganum,25.0 in r-sparganum and 215.0 in adult worms, so that the maximum activity was revealed higher in adults than spargana. As the result from above, we observed that alkaline and acid phosphatases were functioned mainly in the tegument and subtegumental musculature , and the isoxymes of phosphatase were activated differently according to habitat of the parasites. The spargana and adult worms carry out the pafasitism by adapting thenlselves to parasitic circumstance loth these emxymes.

• Current Research on Agriculture and Life Sciences
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• v.3
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• pp.85-91
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• 1985

The change of acid-phosphatase in Fuji apples Was investigated in terms of storage temperature and pressure. The firmness, sugar contents, acidity and activity of acid-phosphatase with electrophoretic pattern were studied during storage. The firmness, sugar contents and acidity were decreased during storage. Ratio of decrease was greater at normal temperature than low temperature and normal atmosphere than sub-atmosphere. Acid phosphatase activity of apples was mainly existed cell wall fraction and increased with climacteric rise and decreased later. The activity was higher at normal temperature than low temperature and at atmosphere than sub-atmosphere. The optimal temperature and pH were $45^{\circ}C$ and pH 5.6, respectively. In stability of heat and pH, enzyme solution was stabilized to $30^{\circ}C$ and pH 5-8. Electrophoretic pattern of enzyme solution extracted from sub-atmospheric pressure with low temperature and normal atmospheric pressure with normal temperature yielded two activity bands during storage.

• Applied Microscopy
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• v.3 no.1
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• pp.1-16
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• 1973

A combined cytochemical and electron microscopic study was carried out for the demonstration of acid phosphatase activities in trophozoites of E. histolytica. and E. gingivalis. E. histolytica(YS-27) strain was isolated from liver abscess of 72-year-old man in September 1969, and E. gingivalis (YS-215) strain was collected from gingival crevice of 41-year-old man in January 1972. The amoeba strains were maintained by subculture on diphasic medium, and used throughout the study. The results are summarized as follows; 1. In E. histolytica, the reaction products were distributed evenly over the entire surface of plasma membrane, whereas E. gingivalis showed no activity of acid phosphatase on the plasma membrane, except in the portion of the uroid-like structure. 2. In the cytoplasm, various reaction precipitates were observed in vacuoles of both amoebae; vacuole limiting membrane, vacuole membrane and its contents and lysosome-like structure. Strong enzyme active contents but membrane reaction negative vacuoles were conspicuous in E. gingivalis. Endoplasmic reticulum showed a moderate activity. 3. Granule-like acid phosphatase reaction product was demonstrated in the nucleoplasm of E. gingivalis, but it was negative in E. histolytica.

• The korean journal of orthodontics
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• v.24 no.1 s.44
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• pp.105-114
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• 1994

The movement of teeth during orthodontic treatment requires bone remodeling process of bone formation and bone resolution. To find out the changes occuring in the cell itself, mechanical stress was applied to the cell populations involved in the bone metabolism. Bone tissue cell populations were isolated from fetal rat calvaria and divided into OC and OB groups. Following results were obtained from measuring the changes in acid & alkaline phosphatease activity, cyclic AMP and $PGE_2$ production in time lapse after the application of mechanical stress. 1. In case of the marker enzyme of specific bone tissue cell, acid phosphatase activity was high in OC group and alkaline phosphatase activity was high in OB group. 2. After the mechanical stress was applied, acid phosphatase activity was decreased in both OC and OB groups and alkaline phosphatase activity was increase in OB group. 3. When the mechanical stress was applied for 15, 30 and 60 minutes, the production of $PGE_2$ increased in both OC and OB groups, as the time span increased. 4. When the mechanical stress was applied for 20 and 40 minutes, the production of $PGE_2$ increased in both OC and OB groups, as the time span increased.

• BMB Reports
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• v.30 no.3
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• pp.222-228
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• 1997

Protein phosphatase 2C (PP2C) is one of the four major serine/threonine phosphatases which is dependent on $Mg^{2+}$ for its activity. PP2C was purified from rat liver cytosol and its characteristics were investigated. The substrate employed for routine assay was $[^{32}P]casein$ phosphorylated by PKA. The purification process involved DEAE chromatography, ammonium sulfate fractionation, phenyl sepharose chromatography, sephacryl 5-200 gel filtration, and histone agarose chromatography. The SDS-PAGE of PP2C showed one major single protein band at a position corresponding to a molecular mass of 43 kd and the purification fold was 637. The enzyme showed a pH optimum of 8 and $K_M$ value was $1.9\;{\mu}M$. However, when the substrate was changed to $[^{32}P]histone$, the pH optimum was shifted to 7 and $K_M$ value was $2.3\;{\mu}M.\;Mg^{2+}$ was essential to the enzyme activity and okadaic acid did not exert any inhibitory effect on the enzyme. To examine residue in the active site of PP2C effects of some protein-modifying reagents were tested.

• Journal of Life Science
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• v.7 no.2
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• pp.127-133
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• 1997

The phytase(myo-inositol hexkisphosphate phosphohydrolase ; EC 3.1.3.8) activity was observed only in the homogenate of intestinal mucosa, though the activity of alkaline phisphatase was measurable in various organs. In addition, no protein bands were detected in any other organs on immunoblotting using the anti-90kDa phytase antiserum. Thses results suggest that phytase is specifically present in small intestinal mucosa, and that hydrolysis of phytic acid(inositol-hexakisphosphate) can be allotted for a physiological role of the intestine-specific enzyme. The activities of phytase was increased during development of rat. The 70kDa phytase appeared just after birth, but the 90kDa phytase was not observed until adult period, suggesting that the 90kDa phytase was synthesized in response to weanling.

• Journal of Life Science
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• v.21 no.6
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• pp.893-900
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• 2011

Prostatic acid phosphatase (PAP) is one of the widely used biomarkers in the diagnosis of prostate cancer. It was initially identified in 1935 and is the most abundant phosphatase in the human prostate. PAP is a prostate-specific enzyme that is synthesized in prostate epithelial cells. It belongs to the acid phosphatase group that shows enzymatic activity in acidic conditions. PAP is abundant in prostatic fluid and is thought to have a role in fertilization and oligospermia. It also has a potential role in reducing chronic pain. But one of the most apparent functions of PAP is the dephosphorylation of macromolecules such as HER-2 and PI3P that are involved in the ERK1/2 and MAPK pathways, which in turn leads to inhibition of cell growth and tumorigenesis. Currently, clinical trials using PAP DNA vaccine are underway and FDA-approved immunotherapy using PAP is commercially available. Despite these clinically important aspects, molecular mechanisms underlying PAP regulation are not fully understood. The promoter region of PAP was reported to be regulated by NF-${\kappa}B$, TNF-${\alpha}$, IL-1, androgen and androgen receptors. Here, the features of PAP gene and protein structures together with the function, regulation and roles of PAP in prostate cancer are discussed.

• Applied Biological Chemistry
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• v.31 no.1
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• pp.79-85
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• 1988

The effects of herbicides on biochemical processes in soil environment were studied by examining the effects of the chemical structure of each herbicides on soil enzyme activities and pesticides residue revealed when soil treated with urea was incubated at $28{\pm}1^{\circ}C$ for 56 days. The inhibition effects of herbicides on soil enzyme activites in soil decreased in the order of urea group>dinoseb>propanil>diphenyl eter group>acid amide group for urease, and dinoseb>urea group>diphenyl ether group>acid amide group for L-glutaminase and protease, dinoseb>diphenyl ether group>urea group>acid amide group for phosphatase. Herbicides inhibited the activities of soil enzyme in the early stage of treatment but increased the activities of urease, L-glutaminase and protease in the late stage. When herbicides were treated in soil together with urea the degradation of insecticides was accelerated.

• BMB Reports
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• v.38 no.1
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• pp.58-64
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• 2005

Myo-inositol monophosphate phosphatase (IMPP) is a key enzyme in the phosphoinositide cell-signaling system. This study found that incubating the IMPP from a porcine brain with pyridoxal-5'-phosphate (PLP) resulted in a time-dependent enzymatic inactivation. Spectral evidence showed that the inactivation proceeds via the formation of a Schiff's base with the amino groups of the enzyme. After the sodium borohydride reduction of the inactivated enzyme, it was observed that 1.8 mol phosphopyridoxyl residues per mole of the enzyme dimer were incorporated. The substrate, myo-inositol-1-phosphate, protected the enzyme against inactivation by PLP. After tryptic digestion of the enzyme modified with PLP, a radioactive peptide absorbing at 210 nm was isolated by reverse-phase HPLC. Amino acid sequencing of the peptide identified a portion of the PLP-binding site as being the region containing the sequence L-Q-V-S-Q-Q-E-D-I-T-X, where X indicates that phenylthiohydantoin amino acid could not be assigned. However, the result of amino acid composition of the peptide indicated that the missing residue could be designated as a phosphopyridoxyl lysine. This suggests that the catalytic function of IMPP is modulated by the binding of PLP to a specific lysyl residue at or near its substrate-binding site of the protein.

• Journal of Mushroom
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• v.7 no.3
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• pp.110-114
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• 2009

Sawdust bag cultivation of Shiitake mushroom (Lentinula edodes) is getting increase. The mycelia browning on the substrate surface is important for the stable production. The development of methods for the rapid mycelia browning is quite required. In this study changes in intracellular enzyme during the mycelial browning were investigated to find the rapid mycelia browning. Mycelia of L. edodes was changed into brown color while it grew in agar and liquid media like sawdust substrates. Mycelia of L. edodes was started to change color at 25 days after inoculation and browning was occurred in whole mycelia colony at 30 days and browning was completed at 40 days. The activities of enzymes was evaluated in these periodically color changing mycelia. Laccase activity was highest at 15 days after inoculation on PDB, but it gradually decreased from 15 days. Tyrosinase activity drastically increased in period between 30 days and 40 days while mycelia browning was progressed. The kinds of phosphotase identified by electrophoresis were esterase, acid phosphotase, and alkaline phosphotase. Activities of phosphotase were increased before the initiation of mycelial browning but they were decreased after browning.