• Proceedings of the KSCN Conference
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• 2004.05a
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• pp.437.1-437
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• 2004

The protein, called PTP1B (protein tyrosine phosphatase 1B), joins a list of enzymes that mice are associated with obesity. The purpose of this study was to investigate the effects of PTP1B inhibitors and taurine on blood lipid profiles in adolescents obesity model rats. Three week-old thirty-six male Sprague-Dawley rats were randomly assigned to six groups (high fat diet group; HFD group, high fat diet ＋ taurine group; HF＋TR group, high fat diet＋PTP1B inhibitor A group; HF＋A group, high fat diet＋PTP1B inhibitor B; HF＋B group, high fat diet＋PTP1B inhibitor A＋taurine group; HF＋A＋TR group, high fat diet ＋ PTP1B inhibitor B＋taurine group; HF＋B＋TR group).(omitted)

• Korean Journal of Microbiology
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• v.37 no.2
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• pp.158-163
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• 2001

The effect of phosphate on the production of avermectin B1a was studied. Response surface methodology was applied to optimize the concentration of organic nitrogen sources. The portion of B1b in total avermectins was decreased from 5.8% to 3.0% by the addition of 1.5 g/ι inorganic phosphate to the production medium. Among organic nitrogen sources, soybean meal was the most effective on avermectin biosynthesis. Results showed that B1a productivity was increased by 44.8% in a laboratory scale fermenter cultivation of Streptomyces avermitilis YA99-40 through fed-batch process. A maximal B1a productivity was obtained by repeated 30 and 20 g/ι of glucose feeding at 136 and 206 hour, respectively. The B1a productivity was increased by 86.3% and the proportion of B1a in the total avermectins was improved from 38% to 45% with respect to the control process. These results would be very useful for enhancing productivity of B1a in an up-scaled processes.

• Proceedings of the Korean Ceranic Society Conference
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• 2000.10a
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• pp.70.1-70
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• 2000

• Environmental Mutagens and Carcinogens
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• v.19 no.1
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• pp.34-38
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• 1999

Fumonisin B1 is a secondary metabolite of Fusarium moniliforme, a contaminant of corn and corn product. Fumonisin B1 has been shown to be responsible for major toxicological effects of the fungus in rats, horses, and pigs. Fumonisin B1 induced λ DNA fragmentation, which was increased with incubation time, reducing agent NADPH and metal ion (Cu2+). The DNA damage was inhibited by dimethyl sulfoxide (DMSO) or mannitol as radical scavenger for free radicals. DNA fragmentation, induced by fumonisin B1 in the presence of 1 mM NADPH and 0.1 mM CuCl2, was inhibited by 100 mM DMSO. By the in vitro reaction of fumonisin B1 with supercoiled plasmid pBR322 DNA, plasmid DNA was relaxed, eventually linearized in the agarose gel electrphoresis. From rifampicin sensitive E. coli CSH138 in bacterial mutagenesis system, the rifampicin resistant E. coli mutants were obtained by fumonisin B1. These results suggest that fumonisin B1 may be a possible environmental mutagen in bacterial mutagen assay system.

• Journal of Environmental Health Sciences
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• v.22 no.1
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• pp.36-44
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• 1996

A comparison was made of two detection methods(UV absorbence detection and fluorescence detection with pre-column derivatization, with trifluoroacetic acid) coupled with HPLC for the simultaneous determination of aflatoxin $B_1, B_2, G_1$ and $G_2$. A good separation of the four aflatoxins was achieved on a reversed-phase $C_{18}$ column (30 cm x 3.9 mm) with methanol-acetonitrile-water(20+20+60) for absorbence detection or acetonitrile-water(25+75) for fluorescence detection at the flow rate of 1.0 ml/min. The calibration graphs were linear over the ranges 100 ppb-1 ppm for $B_1/G_1$ and 30~300 ppb for $B_2/G_1$ with absorbence detection, and 1~500 ppb for $B_1/G_1$ and 0.3~150 ppb for $B_2/G_2$ with fluorescence detection. The correlation coefficients were greater than 0.94 and 0.99 for absorbance detection and for fluorescence detection, respectively. The detection limit was 100 ng for $B_1/G_1$ and 30 ng for $B_2/G_2$ with absorbence detection, and 1 ng for $B_1/G_1$ and 0.3 ng for $B_2/G_2$ with fluorescence detection. Recovery rates of aflatoxin $B_1, B_2, G_1$ and $G_2$ added to yeast-extract sucrose broth medium were 66.6%, 59.4%, 67.5% and 59.2%, respectively, for absorbence detection and 82.9%, 71.5%, 80.0% and 69.3%, respectively, for fluorescence detection. The four aflatoxins in culture medium were quantitatively detected by the two methods. The aflatoxins in the rice sample were not detected the absorbence detection method, but were below 10 ppb using the fluorescence detection method. Analysis of aflatoxins by both the absorbence and fluorescence methods coupled with HPLC showed acceptable linearity and good recovery. The absorbence detection was less timeconsuming and safer for treatment. The fluorescence detection was more elective and sensitive though elevated $B_1$ and $G_1$ contents were determined from the TFA-induced conversion of $B_1$ to $B_{2a}$ and $G_1$ to $G_{2a}$.

• Archives of Pharmacal Research
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• v.15 no.3
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• pp.263-268
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• 1992

In order to evaluate the antimicrobial effect of 2, 3-disubstitued-1, 4-naphtoquinone derivatives we newly synthesized several 2-bromo-3-(substituted)-1, 4 naphthoquninones. Amination reaction of 2, 3-dihalo-1, 4 naphthoquinones with aryl and aliphatic amines in ethanol gave 2-halo-3-(N-alkyl or N-aryl)1, 4-naphtoquinone derivatives (1a, b-10a, b) i 60% 90%) yield. These derivatives subjected to antibacterial and antifungal activities. in vitro, against Bacilllus subtilis ATCC 6633 Candida albicans 10231 and local, Psudomonas aeruginosa NCTC10490, Staphylococcus aureus ATCC 6538p. Escherichia coli NIHJ Aspergillus niger KCTC 1231, Tricophyton mentagrophytes KCTC 6085. Among these derivatives 1b, 6b and 7a showed the potent antibacterial activities 1b, 8b and 9b have derivatives, 1b, 6b and 7a showed the potent antibacterial activities. 1b, 8b and 9b have the antifungal activities. 1b is most effective in preventing the growth of Bacillus subtilis and Psudomonas aeruginosa. Candida albicans. Aspergillus niger. Tricophyton mentagrophytes. The several of these compounds demonstrated a broad spectrum of activities in vitro.

• YAKHAK HOEJI
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• v.41 no.6
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• pp.789-796
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• 1997

The purpose of this study was to determine the effect of sulfinpyrazone on fumonisin $B_1$-induced elevation of free sphingoid bases in LLC-$PK_1$ cells. Fumonis ins are a family of mycotoxins produced by the fungi Fusarium moniliforme which is common contaminant in corn. Fumonisins are also potent inhibiors of sphingosine and sphinganine N-acyltransferases (ceramide synthases), key enzymes in sphingolipid metabolism resulting in the elevation of free sphinganine. The cytosolic concentration of fumonisin B1 was known to be closely proportional to the elevation of free sphinganine in LLC-PK1 cells [Yoo, H.-S., Norred, W.P., Wang, E., Merrill, A.H., Jr., and Riley, R.T. (1992) Toxicol. Appl.Pharmacol. 114. 9-15]. Sulfinpyrazone, an anion transport inhibitor, reduced the elevated level of free sphinganine resulting from fumonisin B1 inhibition of de novo sphingolipid biosynthesis. Fumonisin B1 at a concentration of 20${\mu}$M showed approximately 120pmol/$10^6$ cells relative to 3-10pmol/$10^6$ cells in control cultures, and sulfinpyrazone at a concentration of 200${\mu}$M partially reversed the increased level of free sphinganine induced by fumonisin $B_1$ down to normal level after exposure to fumonisin $B_1$ for 8 to 24hr. However, the reduced effect of sulfinpyrazone on the fumonisin $B_1$-induced elevation of intracellular sphinganine was not shown after 24hr. Fumonisin $B_1$ exposure to LLC-PK1 cells for 36 and 48hr showed approximately 74 and 80pmol per $10^6$ cells relative to 82 and 76pmol,respectively, in fumonisin $B_1$ plus sulfinpyrazone-treated cultures. Sulfinpyrazone-induced less elevation of free sphinganine in confluent cells after exposure to fumonisin $B_1$ suggested that either sulfinpyrazone may block the availability of fumonisin $B_1$ to cells or act on the fumonisin $B_1$ interaction with ceramide synthase.

• Journal of Embryo Transfer
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• v.28 no.1
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• pp.57-61
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• 2013

Microtubule-associated protein 1B (MAP1B), a member of MAP1 family, plays a key role in neuronal development. MAP1B binds to many kinds of proteins directly or indirectly. This study was performed to investigate whether MAP1B interacts with GAPDH in bovine follicles using immunoprecipitation (IP) with Western blot analysis and immunohistochemisty. The mRNA expressions of MAP1B and glyceraldehydes 3-phosphate dehydrogenase (GAPDH) were down-regulated in bovine follicular cystic follicles (FCF). In parallel with the mRNA levels, their protein levels were also down-regulated in FCFs. In addition, MAP1B and GAPDH were co-localized at the cytoplasm of follicles. IP with Western blot analysis showed that MAP1B bound to GAPDH in normal follicles, but their binding was absent in FCFs, suggesting a low level of MAP1B and/or GAPDH expressions in FCFs. Taken together, these results suggest that MAP1B interacted with GAPDH may play a role in bovine follicle development, and that GAPDH does not function always as a loading control in bovine follicles.

• Journal of the Korean Chemical Society
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• v.43 no.3
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• pp.302-306
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• 1999

The 1,3-dipolar cycloaddition reaction of the quinoxaline 4-oxide 10 with 2-chloroacrylonitrile gave the 2,3-dihydro-lH-1,2-diazepino[3,4-blquinoxalines lla, b, respectively, which were converted into the 2,3,4,6-tetrahydro-lH-l,2-diazepino[3,4-b]quinoxaline 12. The reaction of compound lla with selenium dioxide in acetic acid/water resulted in ring transformation to give the 1,4-dihydro-4-oxopyridazino[3,4-blquinoxaline 13.

• Journal of Marine Bioscience and Biotechnology
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• v.2 no.4
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• pp.230-233
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• 2007

Protein tyrosine phosphatase 1B (PTP1B) acts as a negative regulator of insulin signaling, and selective inhibition of PTP1B has served as a potential drug target for the treatment of type 2 diabetes. As part of our searching for PTP1B inhibitors from natural products, the extracts of marine microorganisms were screened for the inhibitory effects on the activity of protein tyrosine phosphatase 1B (PTP1B). Among the tested 304 extracts, 29 extracts exhibited inhibition rate ranging 40.1 - 83.6 % against PTP1B at the concentration level of $30{\mu}g/mL$.