• Proceedings of the SCSK Conference
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• 2003.09a
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• pp.660-671
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• 2003

A chemical investigation of Peucedanum praeruptorum has resulted in the isolation of 3 khellactone derivatives, which have inhibitory effects on melanogenesis in B16 mouse melanoma cell lines. The khellactone derivatives were isolated from the crude extract of the roots of Pecedanum praeruptorum by a combination of adsorption chromatography and HPLC. The structures of isolated compounds were identified as 3', 4'-diangeloyl-cis-khellactone, 3'-angeloyl-4'-senecioyl-cis-khellactone and, 3', 4'-disenecioyl-cis-khellactone by $^1$H NMR, $^{13}$ C NMR and mass spectral studies and by comparisons of spectral data with reported literatures. These khellactone derivatives can be a good candidate for new skin whitening agent due to its strong inhibitory activity and safety.

• Korean Journal of Microbiology
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• v.23 no.1
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• pp.13-19
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• 1985

Acc I endonuclease has been isolated from 300g (wet weight) cells of Acinetobacter calcoaceticus. The cells were broken by using French press at 20, 000p.s.i. After ammonium sulfate fractionation, the enzyme was further purified by heparin agarose, DEAE-sephades, Affi.-gel Blue, phosphocellulose, and hydroxylapatite column chromatography. The purified Acc I endonudlease has a single polypeptide species and its subunit molecular weight was 45,000 ${\pm}$ 1,000 daltons as judged by 10% SDS-polyacrylamide gel electrophoresis. The isolated enzyme was essentially free of contaminating nucleases as judged by homochromatography by using a $^{32}P-labeled$ oligonucleotide. The enzyme showed maximum activity at pH values between 8.0 and 11.0 and in the presence of $MgCl_2$. Acc I endonuclease was maximally active in the absence of NaCl and was completely inhibited at 200 mM NaCl.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.672-675
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• 2000

E.coli ATCC 33456 has relatively higher activity of Cr(VI) reduction than other microorganism. The purpose of this research is cloning of Cr(V) reductase from E.coli ATCC 33456. Using colony and southern hybridization, we selected two condidates. Among candidates, pNCR9 is higher Cr(VI) reduction activity than E.coli ATCC 33456. Purified Cr(VI) reductase antibody was reacted at estimated 42Kda protein band of candidate's crude extract on 12% SDS-PAGE. This results showed cloned gene's product is very similar to purified Cr(VI) reductase from E.coli ATCC 33456.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.575-578
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• 2000

The N-acetylneuraminate lyase(NALase) from Escherichia coli was cloned and it was compared to that from Haemophilus influenzae and Clostridium perfringens. NALase from E. coli was expressed in very high level(about 6U/mg). The ManNAc Km value of three enzymes was almost the same. Pyruvate inhibited from H. influenzae was inhibited by GlcNAc in lower level than the others. The crude extract has about 30 times more activity than the cell for the substrate and product diffusion limit problem. The pH stability of three enzymes at pH 11 was also checked for its importance in the direct synthesis of Neu5Ac from GlcNAc and pyruvate at high alkaline condition.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.3
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• pp.241-245
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• 1991

A polyphenol oxidase from the crude extract of Aster scaber was partially purified by (NH4)2 SO4 precipitation and subsequent Sephadex G-150 chromatography. The final preparation showed five peaks of enzyme activity. Optimum pH and temperature for the activity of polyphenol oxidase were 7.0 and $30^{\circ}C$, respectively. Enzyme activity was stable at $40^{\circ}C$ for 5min in pH 7.0 reaction mixture but ceased completely at $60^{\circ}C$ for 30min and $70^{\circ}C$ for 5min at pH 7.0. The olyphenol oxidase has good activity acid but was inactive on DL-depa. The apparent Km for catechol was about 17.6mM.

• KSBB Journal
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• v.31 no.4
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• pp.200-207
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• 2016

In the present study, antioxidant activity of crude extract and its solvent-partitioned subfractions (n-hexane, 85% aqueous methanol, n-butanol, and water) obtained from Atriplex gmelinii was investigated using several different antioxidant assays. The tested samples possessed different antioxidant and radical-scavenging activities in different assays. n-butanol fraction showed the most potent radical-scavenging activity on reducing power while 85% aqueous methanol fraction exhibited the highest radical-scavenging activity on DPPH radicals and intracellular reactive oxygen species (ROS). On the otherhand, n-BuOH and 85% aqueous methanol revealed the similar inhibitory effect on peroxynitrite-scavenging and genomic DNA oxidation. These results suggest that the Atriplex gmelinii can be used as the valuable source for developing a natural antioxidant.

• Journal of Ecology and Environment
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• v.33 no.2
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• pp.141-147
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• 2010

This study compared the antimicrobial activity and chemical composition of two plants used as "Injin" (Korean herbal medicine), namely, Injinho (Artemisia capillaris Thunberg) and Haninjin (Artemisia iwayomogi Kitamura). The ethyl acetate and ether fractions of crude methanol extracts from A. capillaris and A. iwayomogi were tested against three grampositive bacteria (Bacillus cereus, Bacillus subtilis, Staphylococcus aureus), two gram-negative bacteria (Escherichia coli, Pseudomonas fluorescens), and a yeast (Saccharomyceus cerevisiae). The antimicrobial activity of the ethyl acetate and ether fraction of both plants was strong, but that of A. iwayomogi extracts was higher than that of A. capillaris extract for the microbes tested. The minimum inhibitory concentration of the ether and ethyl acetate fraction of A. iwayomogi was highest for P. fluorescens and lowest for S. aureus and E. coli. We analyzed the chemical composition of the ethyl acetate fraction of A. capillaris and A. iwayomogi using gas chromatography-mass spectrometry. The main components of A. capillaris and A. iwayomogi were escoparone (86.82%) and scopoletin (20.47%), respectively.

• BMB Reports
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• v.35 no.6
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• pp.576-582
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• 2002

Collagenase from the internal organs of a mackerel was purified using acetone precipitation, ion-exchange chromatography on a DEAE-Sephadex A-50, gel filtration chromatography on a Sephadex G-100, ion-exchange chromatography on DEAE-Sephacel, and gel filtration chromatography on a Sephadex G-75 column. The molecular mass of the purified enzyme was estimated to be 14.8 kDa by gel filtration and SDS-PAGE. The purification and yield were 39.5-fold and 0.1% when compared to those in the starting-crude extract. The optimum pH and temperature for the enzyme activity were around pH 7.5 and $55^{\circ}C$, respectively. The $K_m$ and $V_{max}$ of the enzyme for collagen Type I were approximately 1.1 mM and 2,343 U, respectively. The purified enzyme was strongly inhibited by $Hg^{2+}$, $Zn^{2+}$, PMSF, TLCK, and the soybean-trypsin inhibitor.

• BMB Reports
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• v.30 no.4
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• pp.274-279
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• 1997

Acetolactate synthase (ALS) catalyzes the first common step in the biosynthesis of branchedchain amino acids, valine, leucine, and isoleucine. ALS is the target site for several structually diverse classes of herbicides including sulfonylureas, imidazolinones. and triazolopyrimidines. We have purified ALS from etiolated barley shoots to homogeneity. The five major purification steps are ammonium sulfate fractionation, DEAE anion exchange, hydroxylapatite, Bio-Gel A gel filtration, and low pressure Mono-Q chrornatoqraphy. Approximately 170-fold purification was achieved and the yield was 0.45% of initial activity in the crude extract. Both SDS-PAGE and Western blot analysis showed a single polypeptide of ALS with an apparent molecular mass of 64 kDa. The result of nondenaturing gel electrophoresis with activity staining indicated that the molecular mass of its native form is approximately 225 to 250 kDa. The values of $K_m$ for pyruvate. pl. and optimum pH of ALS were determined to be 2.0 mM, 5.2. and 7.0. respectively Feedback inhibition studies showed that ALS is more susceptible to leucine than valine. And $IC_{50}$ value of Cadre, a class of irnidazolinones, is about $1.5\mu{M}$ for ALS.

• Korean Journal of Pharmacognosy
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• v.33 no.4 s.131
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• pp.395-398
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• 2002

A chemical investigation of Peucedanum praeruptorum has resulted in the isolation of 3 khellactone derivatives, which have inhibitory effects on melanogenesis in Bl6 mouse melanoma cell lines. The khellactone derivatives were isolated from the crude extract of the roots of Pecedanum praeruptorum by a combination of adsorption chromatography and HPLC. The structlues of isolated compounds were identified as 3',4'- diangeloyl-cis-khellactone, 3'-angeloyl- 4'- senecioyl-cis-khel- lactone and,3', 4'-disenecioyl-cis-khellactone by $^1H\;NMR$, $^{13}C\;NMR$ and mass spectral studies and by comparisons of spectral data with reported literatures.