• Journal of fish pathology
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• v.27 no.1
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• pp.25-33
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• 2014

Hydrolase activities of excretory-secretory products (ESP) and somatic extracts (SE) from Anisakis simplex sensu stricto (s.s.) and Anisakis pegreffii larvae were investigated by using API ZYM kit. In esterase group, acid phosphatase showed high activity from both of A. simplex (s.s.) and A. pegreffii. Esterase (C4) showed activity only from SE and A. simplex (s.s.) showed higher activity than A. pegreffii. Alkaline phosphatase, acid phosphatase and naphthol-AS-BI-phosphohydrolase showed higher activity in 3rd stage larvae than in 4th stage larvae of both species. In aminopeptidase group, only leucine arylamidase showed remarkable activity in SE of both anisakid species, and A. simplex (s.s.) SE showed higher activity than A. pegreffii SE. In glycosidase group, N-acetyl-${\beta}$-glucosaminidase, ${\alpha}$-mannosidase, ${\alpha}$-fucosidase showed higher activity in A. simplex (s.s.) than A. pegreffii, and 4th larvae showed higher activity than 3rd larvae. These differences in hydrolase activity of anisakid nematodes larvae are thought to be due to different metabolism such as growth, moulting, digestion and feeding.

• Korean Journal of Breeding Science
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• v.42 no.5
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• pp.455-462
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• 2010

Purple acid phosphatase is important for phosphorus remobilization in plants, but its role in plant adaptation to low phosphorus availability is not known. The cDNA encoding O. sativa purple acid phosphatase (OsPAP1) has 1008 bp with an open reading frame of 335 amino acid residues. The amino acid sequence of OsPAP1 cDNA shows of 50-51% identity with other plant purple acid phosphatases. OsPAP1 was expressed in rice plants and in cell cultures in the absence of phosphate ($P_i$). The expression was organ-specific with the strongest expression in $P_i$-deprived roots. Functional expression of the OsPAP1 gene in the transgenic Arabidopsis line was confirmed by northern and western blot analysis. OsPAP1 overexpression lines had higher phosphatase activity than wild-type. Overexpression of OsPAP1 in Arabidopsis plants resulted in increased Pi accumulation under Pi sufficient condition. These results show that the OsPAP1 gene represents more efficient $P_i$ uptake and can be used to develop new transgenic dicotyledonous plants.

• 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.

• 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.

• BMB Reports
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• v.28 no.1
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• pp.12-16
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• 1995

The branched-chain ${\alpha}$-keto acid dehydrogenase (BCKAD) complex is a rate limiting enzyme which catalyzes the oxidative decarboxylation of branched-chain ${\alpha}$-keto acids. Numerous studies have suggested that BCKAD is subject to covalent modification in vitro via phosphorylation and dephosphorylation, which are catalyzed by a specific kinase and phosphatase, respectively. The biggest difficulty in the assay of BCKAD activity is to arrest the interconversion between the active and inactive forms. BCKAD activity was determined from fresh rat heart and liver tissues using homogenizing and assay buffers containing inhibitors of phosphatase and kinase. The results suggest that a radiochemical assay using ${\alpha}$-keto[1-$^{14}C$]-isovalerate as a substrate for the enzyme can be applied as a reliable method to determine in vitro enzyme activity with arrested interconversion between the active and inactive forms of the BCKAD complex.

• The Journal of the Korean dental association
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• v.13 no.1
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• pp.37-45
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• 1975

• The Korean Journal of Zoology
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• v.22 no.2
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• pp.67-81
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• 1979

Eelctron microscopic cytochemical methods reveal that acid phosphatase activity appears exclusively in vacuoles surrounding established symbiotes. However, copius amounts of acid phosphatase reaction product are visible between and around some of the degenerating symbiotes in the amebae after treatment of chloramphenicol. It is thought that bacteriostasis by chloramphenicol has served to lost the symbiotic interference to intracellular digestion by the ameba and possibly phodphatase enxymes have been implicated in phagocytosis and intracellular digestion of the symbiotic bacteria.

• Clinical and Experimental Reproductive Medicine
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• v.9 no.1_2
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• pp.55-68
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• 1982

The present investigation has been undertaken to understand the mechanism of implantation process, by demonstrating the role of ovarian steroids in connection with phosphatase activity in the differentiation of uterine endometrium for implantation. The results obtained are as followings: The differentiation of the uterine endometrial tissue was closely influenced by the ovarian steroid hormones; at first, 17${\beta}$-estradiol initiated the differentiation of the uterine luminal and glandular epithelial cells, and then progesterone induced differentiation of stromal cells, and thereby two steroids maintain decidualization of the uterine tissues. We observed that the phosphatase activities seem to be dependent upon the ovarian steroids; that is the activity showed higher level in progesterone treated group than in estradiol treated one, and the highest activity was found in the group treated with both estradiol and progesterone. Acid phosphatase showed the highest activity whereas alkaline phosphatase showed the lowest in the rat uterine endometrium during early pregnancy.

• Animal cells and systems
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• v.14 no.2
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• pp.73-81
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• 2010

In this study, monoclonal antibodies against lysosomal acid phosphatase (LAP) of a salamander, Hynobius leechii, were used to determine the spatial and temporal expression of the LAP in the regenerating limbs. The Western blot and immunohistochemical analysis in the limb regeneration revealed that LAP was highly expressed at the dedifferentiation stage, especially in the wound epidermis and dedifferentiating limb tissues such as muscle and cartilage. With RA treatment, the LAP expression became upregulated in terms of both level and duration in the wound epidermis, blastemal cell and dedifferentiating limb tissues. In addition, in situ activity staining of LAP showed a similar result to that of immunohistochemistry. Thus, the activity profile of LAP activity coincides well with the expression profile of LAP during the dedifferentiation period. Furthermore, to examine the effects of lysosomal enzymes including LAP on salamander limb regeneration, lysosome extract was microinjected into limb regenerates. Interestingly, when the lysosome extract was microinjected into limb regenerates with a low dose of RA($50\;{\mu}g/g$ body wt.), skeletal pattern duplication occurred frequently in the proximodistal and transverse axes. Therefore, lysosomal enzymes might cause the regenerative environment and RA plays dual roles in the modification of positional value as well as evocation of extensive dedifferentiation for pattern duplication. In conclusion, these results support the hypothesis that dedifferentiation is a crucial event in the process of limb regeneration and RA-evoked pattern duplication, and lysosomal enzymes may play important role(s) in this process.

• Korean Journal of Food Science and Technology
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• v.19 no.5
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• pp.441-445
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• 1987

The subcellular distribution of lipoxygenase in germinating soybean seeds (Glycine max[L.] AmSoy) was investigated by using differential centrifugation and sucrose density gradient fractionation. Most of lipoxygenase -1 and -2/3 activities was present in the supernatant fraction after differential centrifugation of homogenates prepared from three-day-old seedlings; only 1.5% of lipoxygenase activity remained in particulate fractions. The results of a sucrose density gradient fractionation (three-day-old) showed that the lipoxygenase activity coincided with acid phosphatase at the densities of 1.19, 1.23, $1.25g/cm^3$, even though most of lipoxygenase and acid phosphatase activities appeared in supernatant fractions. There was no indication that mitochondria contained any lipoxygenase activity, and it does not appear that glyoxysomes and ER contained any lipoxygenase activity either.