• 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.

• Mass Spectrometry Letters
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• v.9 no.3
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• pp.67-72
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• 2018

Alkaline phosphatase (AP) is a membrane-bound glycoprotein that is widely distributed in the plasma membrane of cells of various organs and also found in many organisms from bacteria to humans. The complete amino acid sequence and three-dimensional structure of human placental alkaline phosphatase have been reported. Based on the literature data, AP consists of two presumptive glycosylation sites, at Asn-144 and Asn-271. However, it only contains a single occupied N-linked glycosylation site and no occupied O-linked glycosylation sites. Hydrophilic interaction chromatography (HILIC) has been primarily employed for the characterization of the glycan structures derived from glycoproteins. N-glycan structures from human placental alkaline phosphatase (PLAP) were investigated using HILIC-Orbitrap MS, and subsequent data processing and glycan assignment software. 16 structures including 10 sialylated N-glycans were identified from PLAP.

• 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 Veterinary Research
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• v.15 no.2
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• pp.233-240
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• 1975

Glycogen and alkaline phosphatase were studied histochemically in the placenta of the golden hamster (Mesocricetus auratus). The results were summarized as followings: 1. The histochemical distribution of glycogen and alkaline phosphatase was described in the various cells of both the placenta and uterus from implantation (5 days past coitum) parturition. 2. Glycogen appeared in the extraembryonic ectorm of the implanting ovum and increased gradually in the ectoplacental cone with the development of the placenta. 3. Glycogen granules began to accumulate in the labylinthine trophoblast of chorioallantoic placenta at 10.5 days and in the endodermal cells the visceral yolk sac sac at 10 days, respectively, and in these both cells glycogen increased gradually until the 13 days post coitum and after this time decreased progressively. 4. Alkaline phosphatase activity was high in the labyrinth, junctional zone and decidua, but was not observed in the yolk sac and trophospongium.

• Microbiology and Biotechnology Letters
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• v.13 no.4
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• pp.403-408
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• 1985

Enhancement of surfactant on release of secretory enzyme, such as $\alpha$-amylase, acid phosphatase and alkaline phosphatase, was investigated during submerged culture of Rhizopus oryzae. Morphological changes of colony was occured; small pelletal form in 0.18mM of sodium dodecyl sulfate, pulpy form in 0.48mM of sodium deoxycholate, and filamentous form in absence of surfactant. It. Supplement of sodium dodecyl sulfate induced 9 times increasing activity of $\alpha$-amylase and that of acid phosphatase 25 times in cultural fluids. Alkaline phosphatase was increased 11 times in cultural fluid and also stimulated in cytoplasm with supplement of sodium deoxycholate.

• Journal of the East Asian Society of Dietary Life
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• v.23 no.1
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• pp.39-43
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• 2013

Carthamus tinctorius L. and Eucommia umoides Oliver are often used in traditional herbal medicines for reducing damage to the liver, kidney, bone and muscle. In the present study, we investigated cell viability and alkaline phosphatase activity in the human osteoblast-like MG-63 cell line with methanol extracts of Carthami Semen (CS) and Eucommiae Cortex (EC) alone or in a mixture (CS+EC). Osteoblast cell viability was evaluated using the MTS assay and alkaline phosphatase activity assays. The cell viability and alkaline phosphatase activity significantly increased in MG-63 osteoblast cells treated with the CS+EC mixture. These findings suggest the CS+EC mixture may have beneficial effects on bone health through the proliferation of osteoblast cells.

• The Korean Journal of Zoology
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• v.16 no.2
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• pp.139-145
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• 1973

The activity of acid and alkaline phosphatases of pine moth, Dendrolimus spect abilis Butler was measured in a serier of developmental stages ranging from the larva to the adult. The activity of both enzymes increased gradually with age of larvae, and then decreased in the prepupal stage. Acid enzyme was at a maximum in the pupal early stage and alkaline enzyme in the 8th instar larva, respectively. And in the prepupal stage there were no significant differences between both acid and alkalnie phosphatases. However, their activities were far lower than in the 8th instar larva. In the pupal early stage there occurs a increase in the acitivity of acid enzyme followed by a decrease in the pupal later stage, and in the adult stage its activity increased again.

• YAKHAK HOEJI
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• v.37 no.6
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• pp.571-576
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• 1993

The substrate specificity of the purified rabbit plasma alkaline phosphatase (ALPase) was determined towards a extended range of potential substrates including relatively simple phosphate derivatives as p-NPP and indolyl phosphate, and several synthetic peptides and phosphoproteins. These results further estabilish the broad substrate specificity of these circulating enzymes. Interestingly, the plasma ALPase preferentially dephosphorylates Thr over Ser residues, as demonstrated with a series of synthetic peptides. The latter result is in contradiction to the behaviour of the tissue ALPase, which is thought to the ultimate source of plasma ALPase, and open therefore new perspectives with respective to the origin and "solubilisation" processes of these enzymes. Dephsphrylation of protein substrates by endogenous and isolated plasma ALPases indicates that ALPase probably displays protein phosphatase activity in vivo.

• The Korean Journal of Mycology
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• v.25 no.2 s.81
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• pp.85-90
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• 1997

The Isozyme activities of Lentinula edodes were studied as a preliminary study for genetic analysis after protoplast fusion. The presence of peroxidase, esterase, superoxide dismutase, acid phosphatase, alkaline phosphatase, alcohol dehydrogenase and ${\alpha}-amylase$ was examined. An intracellular buffer-soluble protein from the mycelia was used for enzyme analysis on nondenaturing polyacrylamide gels. The auxotrophs of Lentinula edodes were positive for peroxidase, esterase, superoxide dismutase and acid phosphatase. However, alkaline phosphatase, alcohol dehydrogenase and ${\alpha}-amylase$ were not detected. The esterase and peroxidase were not affected by the various culture age. Isozyme identification may be a useful tool after protoplast fusion.

• Ocean Science Journal
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• v.40 no.4
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• pp.183-190
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• 2005

We investigated the seasonal variability of tree alkaline phosphatase activity in seawater and alkaline phosphatase hydrolysable phosphorus (APHP) at 3 stations in Hiroshima Bay using alkaline phosphatase extracted from the dinoflagellates Alexandrium tamarense and Gymnodinium catenatum. The dissolved inorganic phosphorus (DIP) was lower than $1\;{\mu}M$ all samples; the lowest values were in May. The amount of APHP was high at the surface and bottom waters of all stations in May, showing DIP-depleted conditions. In August and November, the amount of APHP was much less than the amount of APHP in May, indicating that the availability of dissolved organic phosphorus (DOP) for these species was low and/or uptake during the dinoflagellate blooming might have occurred in the area. The results obtained from short-term variations of AP activity might suggest that the growth of dinoflagellates in this season may be partly supported by the AP produced by other diatoms.