• Parasites, Hosts and Diseases
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• v.57 no.6
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• pp.639-645
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• 2019

In the present study, a Spirometra species of Tanzania origin obtained from an African leopard (Panthera pardus) and spotted hyena (Crocuta crocuta) was identified based on molecular analysis of cytochrome c oxidase I (cox1) and NADH dehydrogenase subunit I (nad1) as well as by morphological observations of an adult tapeworm. One strobila and several segments of a Spirometra species were obtained from the intestine of an African male leopard (Panthera pardus) and spotted hyena (Crocuta crocuta) in the Maswa Game Reserve of Tanzania. The morphological characteristics of S. theileri observed comprised 3 uterine loops on one side and 4 on the other side of the mid-line, a uterine pore situated posterior to the vagina and alternating irregularly either to the right or left of the latter, and vesicular seminis that were much smaller than other Spirometra species. Sequence differences in the cox1 and nad1 genes between S. theileri (Tanzania origin) and S. erinaceieuropaei were 10.1% (cox1) and 12.0% (nad1), while those of S. decipiens and S. ranarum were 9.6%, 9.8% (cox1) and 13.0%, 12.6% (nad1), respectively. The morphological features of the Tanzania-origin Spirometra specimens coincided with those of S. theileri, and the molecular data was also consistent with that of S. theileri, thereby demonstrating the distribution of S. theileri in Tanzania. This places the leopard (Panthera pardus) and spotted hyena (Crocuta crocuta) as new definitive hosts of this spirometrid tapeworm.

• Bulletin of the Korean Chemical Society
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• v.23 no.11
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• pp.1640-1642
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• 2002

• The Plant Pathology Journal
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• v.16 no.2
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• pp.63-69
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• 2000

No Abstract.See Full-text

• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.239.1-239
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• 1995

• Bulletin of the Korean Chemical Society
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• v.22 no.1
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• pp.13-14
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• 2001

• Molecules and Cells
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• v.46 no.8
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• pp.473-475
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• 2023

• YAKHAK HOEJI
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• v.17 no.1
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• pp.1-8
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• 1973

The pharmacological activities of paeoniflorin abtained from paeony roots, F$_M$100 from glycyrrhiza roots, crude saikosides from bupleurum roots, crude platycodin from platycodon roots, and bothj of ginsenoside Rb and ginsenoside Rg series from ginseng roots were investigated. Paeoniflorin, F$_M$ 100, crude saikosides, and crude platycodin exhibited sedative antipyretic, anlagesic and anti-ulcerative actions. In addition, crude saidosides and crude platycodin showed antitusaive and the potent anti-inflammatory action. An expectorant action was also observed with crude platycodin. These results coincided with the clinical applications of the aforementioned oriental medicinals. It also should be noted that crude saikosides nad crude platycodin are preferable to the other steroidal nad nonsteroidal drugs as an anti-inflammatory agent, because the drugs aggravate the digestive ulcer. In ginseng, G No3. and GNS frctions out of ginsenoside Rb series hsowed stimulant and antifatigue actions. The synergistic effects identified between paeoniflorin and F$_M$ 100 on the various pharmacological activities, have verified the reasonability of combined uses of two oriental drugs as Jakyak Gaqmcho-Tang.

• Journal of Microbiology
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• v.42 no.1
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• pp.20-24
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• 2004

Cloned myo-inositol-1-phosphate synthase (INOS) of Drosophila melanogaster was expressed in Escherichia coli, and purified using a His-affinity column. The purified INOS required NAD$\^$+/ for the conversion of glucose-6-phosphate to inositol-1-phosphate. The optimum pH for myo-inositol-1-phosphate synthase is 7.5, and the maximum activity was measured at 40$^{\circ}C$. The molecular weight of the native enzyme, as determined by gel filtration, was approximately M$\_$r/ 271,000${\pm}$15,000. A single subunit of approximately M$\_$r/ 62,000${\pm}$5,000 was detected upon SDS-polyacrylamide gel electrophoresis. The Michaelis ($K_{m}$) and dissociation constants for glucose-6-phosphate were 3.5 and 3.7 mM, whereas for the cofactor NAD$\^$+/ these were 0.42 and 0.4 mM, respectively.

• BMB Reports
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• v.45 no.2
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• pp.91-95
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• 2012

Glutamate dehydrogenase from axenic bacterial cultures of a new microorganism, called GWE1, isolated from the interior of a sterilization drying oven, was purified by anion-exchange and molecular-exclusion liquid chromatography. The apparent molecular mass of the native enzyme was 250.5 kDa and was shown to be an hexamer with similar subunits of molecular mass 40.5 kDa. For glutamate oxidation, the enzyme showed an optimal pH and temperature of 8.0 and $70^{\circ}C$, respectively. In contrast to other glutamate dehydrogenases isolated from bacteria, the enzyme isolated in this study can use both $NAD^+$ and $NADP^+$ as electron acceptors, displaying more affinity for $NADP^+$ than for $NAD^+$. No activity was detected with NADH or NADPH, 2-oxoglutarate and ammonia. The enzyme was exceptionally thermostable, maintaining more than 70% of activity after incubating at $100^{\circ}C$ for more than five hours suggesting being one of the most thermoestable enzymes reported in the family of dehydrogenases.

• KSBB Journal
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• v.11 no.4
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• pp.489-496
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• 1996

Metal dispersed carbon paste electrodes were fabricated, and their electrochemical properties were investigated. Among various metal dispersed carbons, platinum-dispersed carbon paste electrode showed most efficient electrocatalytic characteristics. The overpotential for the oxidation of NADH was significantly lowered in the platinum-dispersed carbon paste electrode, and catalytic current was also enhanced. Based on these electrocatalytic observations, L-lactate biosensor using L-lactate dehydrogenase was constructed to evaluate its performance in terms of sensitivity and stability.