• 한국약용작물학회:학술대회논문집
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• 2008.05a
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• pp.67-68
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• 2008

• Journal of Ginseng Research
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• v.33 no.4
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• pp.249-255
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• 2009

The oxidation of glycolate to glyoxylate, a key step in plant photorespiration, is carried out by the peroxisomal flavoprotein glycolate oxidase (EC 1.1.3.15). To investigate the altered gene expression and the role of GOX in ginseng plant defense system, a cDNA clone containing a GOX gene designated as PgGOX was isolated and sequenced from Panax ginseng. The cDNA was 692 nucleotides long and have an open reading frame of 552 bp with a deduced amino acid sequence of 183 residues. A GenBank BlastX search revealed that the deduced amino acid of PgGOX shares a high degree homology with the Glycine max (95% identity). In the present study we analyzed the expression of PgGOX under various environmental stresses at different times using real time-PCR. The results showed that the expressions of PgGOX increased after various treatments involving salt, light, cold, ABA, SA, and copper treatment.

• Journal of Ginseng Research
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• v.34 no.4
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• pp.288-295
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• 2010

Ginsenosides are the principal components responsible for the pharmacological and biological activities of ginseng. Ginsenoside Rd was transformed into compound K using cell-free extracts of food microorganisms, with Lactobacillus pentosus DC101 isolated from kimchi (traditional Korean fermented food) used for this conversion. The optimum time for the conversion was about 72 h at a constant pH of 7.0 and an optimum temperature of about $30^{\circ}C$. The transformation products were identified by thin-layer chromatography and high-performance liquid chromatography, and their structures were assigned using nuclear magnetic resonance analysis. Generally, ginsenoside Rd was converted into ginsenoside F2 by 36 h post-reaction. Consequently, over 97% of ginsenoside Rd was decomposed and converted into compound K by 72 h post-reaction. The bioconversion pathway to produce compound K is as follows: ginsenoside Rd$\rightarrow$ginsenoside F2$\rightarrow$compound K.

• Journal of Ginseng Research
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• v.34 no.1
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• pp.41-46
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• 2010

Expensive herbs such as ginseng are always a possible target for fraudulent labeling. New mountain ginseng strains have occasionally been found deep within mountain areas and commercially traded at exorbitant prices. However, until now, no scientific basis has existed to distinguish such ginseng from commonly cultivated ginseng species other than by virtue of being found within deep mountain areas. Polymerase chain reaction (PCR) analysis of the internal transcribed spacer has been shown to be an appropriate method for the identification of the most popular species (Panax ginseng) in the Panax ginseng genus. A single nucleotide polymorphism (SNP) has been identified between three newly found mountain ginseng (KGD4, KGD5, and KW1) and already established Panax species. Specific PCR primers were designed from this SNP site within the sequence data and used to detect the mountain ginseng strains via multiplex PCR. The established multiplex-PCR method for the simultaneous detection of newly found mountain ginseng strains, Korean ginseng, and foreign ginseng in a single reaction was determined to be effective. This study is the first report of scientific discrimination of "mountain ginsengs" and describes an effective method of identification for fraud prevention and for uncovering the possible presence of other, cheaper ginseng species on the market.

• 한국약용작물학회:학술대회논문집
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• 2008.05a
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• pp.308-309
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• 2008

• 한국약용작물학회:학술대회논문집
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• 2008.11a
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• pp.123-124
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• 2008

• Proceedings of the Plant Resources Society of Korea Conference
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• 2008.11a
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• pp.72-72
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• 2008

• 한국약용작물학회:학술대회논문집
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• 2008.05a
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• pp.206-207
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• 2008

• 한국약용작물학회:학술대회논문집
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• 2012.05a
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• pp.321-322
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• 2012

• Journal of Physiology & Pathology in Korean Medicine
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• v.22 no.3
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• pp.569-574
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• 2008

The GUE6 was isolated from ethyl acetate fraction of Glycyrrhiza uralensis and confirmed as liquiritin. Liquiritin(LQ) treated with ${\beta}$-glucosidase from plant(Prunus dulcis) and bacteria(Lactobacillus pentosus) crude enzymes. The ${\beta}$-glucosidase activities of crude enzymes were 229.8 U/g(Prunus dulcis) and 19.17 U/ml(Lactobacillus pentosus), respectively. Liquiritin(LQ) biotransformed into liquiritigenin(LQG) by ${\beta}$-glucosidase from crude enzymes. The EtOAc fraction(GUE6) and the converted product were identified as liquiritin and liquiritigenin, by TLC chromatogram, $^{1}H$-NMR and $^{13}C$-NMR.