• Applied Biological Chemistry
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• v.39 no.6
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• pp.482-487
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• 1996

Five barley and two oat varieties grown in Korea were investigated for soluble, insoluble, and total $(1{\to}3)$, $(1{\to}4)-{\beta}-D-glucans$. Total and insoluble ${\beta}-glucans$ after extraction of soluble ${\beta}-glucans$ with water were analyzed, and the soluble ${\beta}-glucans$ were calculated as the difference between total and insoluble ${\beta}-glucans$. The total ${\beta}-glucans$ in whole barleys were in a range of $3.3{\sim}5.6%$(average 4.4%), and those in pearled barleys were In a range of $3.3{\sim}7.1%$(average 5.2%). In whole barleys, on average, 54% of the ${\beta}-glucans$ was soluble and in pearled barley 46%. Whole oats contained $3.1{\sim}4.0%$ total ${\beta}-glucans$, and dehulling increased the groat ${\beta}-glucans$ contents to $4.0{\sim}4.8%$. Oats demonstrated considerably higher ${\beta}-glucans$ solubility of 84% than barley. ${\beta}-Glucans$ in barley and oats were rapidly extracted at the beginning of the extraction and almost all of the ${\beta}-glucans$ were extracted after $2{\sim}3 hr extraction. As extraction temperature increased from $23^{\circ}C$ to $45^{\circ}C$, more soluble ${\beta}-glucans$ were extracted. However, solubility of barley ${\beta}-glucans$ decreased at a relatively high temperature of $65^{\circ}C$. Steam-cooking reduced the analytical solubility of barley and oat ${\beta}-glucans$, while roasting seemed to render the ${\beta}-glucans$ of barley more soluble.

• Molecules and Cells
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• v.26 no.1
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• pp.100-105
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• 2008

Glycogen synthase kinase $3{\beta}$ (GSK $3{\beta}$) is a serine/threonine kinase that phosphorylates substrates such as ${\beta}$-catenin and is involved in a variety of biological processes, including embryonic development, metabolism, tumorigenesis, and cell death. Here, we present evidence that human GSK $3{\beta}$ is associated with Fe65, which has the characteristics of an adaptor protein, possessing a WW domain, and two phosphotyrosine interaction domains, PID1 and PID2. The GSK $3{\beta}$ catalytic domain also contains a putative WW domain binding motif ($^{371}PPLA^{374}$), and we observed, using a pull down approach and co-immunoprecipitation, that it interacts physically with Fe65 via this motif. In addition, we detected co-localization of GSK $3{\beta}$ and Fe65 by confocal microscopy, and this co-localization was disrupted by mutation of the putative WW domain binding motif of GSK $3{\beta}$. Finally, in transient transfection assays interaction of GSK $3{\beta}$ (wt) with Fe65 induced substantial cell apoptosis, whereas interaction with the GSK $3{\beta}$ AALA mutant ($^{371}AALA^{374}$) did not, and we noted that phosphorylation of the Tyr 216 residue of the GSK $3{\beta}$ AALA mutant was significantly reduced compared to that of GSK $3{\beta}$ wild type. Thus, our observations indicate that GSK $3{\beta}$ binds to Fe65 through its $^{371}PPLA^{374}$ motif and that this interaction regulates apoptosis and phosphorylation of Tyr 216 of GSK $3{\beta}$.

• BMB Reports
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• v.46 no.5
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• pp.264-269
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• 2013

Pattern recognition receptors are known to participate in the activation of Prophenoloxidase system. In this study, a 1,3-${\beta}$-D-glucan recognition protein was detected for the first time in Antheraea pernyi larvae (Ap-${\beta}GRP$). Ap-${\beta}GRP$ was purified to 99.9% homogeneity from the hemolymph using traditional chromatographic methods. Ap-${\beta}GRP$ specifically bind 1,3-${\beta}$-D-glucan and yeast, but not E. coli or M. luteus. The 1,3-${\beta}$-D-glucan dependent phenoloxidase (PO) activity of the hemolymph inhibited by anti-Ap-${\beta}GRP$ antibody could be recovered by addition of purified Ap-${\beta}GRP$. These results demonstrate that Ap-${\beta}GRP$ acts as a biosensor of 1,3-${\beta}$-Dglucan to trigger the Prophenoloxidase system. A trace mount of 1,3-${\beta}$-D-glucan or Ap-${\beta}GRP$ alone was unable to trigger the proPO system, but they both did. Ap-${\beta}GRP$ was specifically degraded following the activation of proPO with 1,3-${\beta}$-Dglucan. These results indicate the variation in the amount of Ap-${\beta}GRP$ after specific immune challenge in A. pernyi hemolymph is an important regulation mechanism to immune response.

• YAKHAK HOEJI
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• v.37 no.2
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• pp.158-162
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• 1993

6$\beta$-(trans-3-Aryl-5-oxo-pyrrolidin-2-yl)acetamidopenicillanic acid(7a~7c) and 7$\beta$-(trans-3-Aryl-5-oxo-pyrrolidin-2-yl) acetamidocephalosporanic acid(8a~8c) were synthesized and tested in vitro antibacterial activity. Of these new penicillins exhibited good antibacterial activity against Gram-positive bacteria whereas none of the compounds possessed the activity against Gram-negative bacteria at the concentration tested.

• Journal of Periodontal and Implant Science
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• v.29 no.3
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• pp.645-654
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• 1999

Interleukin-6(IL-6) stimulate osteoclast differentiation. $17{\beta}$-estradiol, 1,25-dihydroxyvitamin $D_3$(1,25-$(OH)_2D_3$) and interleukin-$1{\beta}$ inhibit or stimulate osteoclast differentiation by decreasing or increasing the synthesis of interleukin-6(IL-6) from stromal/osteoblastic cells, respectively. Periodontal ligament(PDL) cells reside between the alveolar bone and the cementum and have osteoblastic characteristics. To estimate the effect of $17{\beta}$-estradiol and 1,25$(OH)_2D_3$ on IL-6 production of PDL cells, PDL cells were treated with $17{\beta}$-estradiol or 1,25-$(OH)_2D_3$ in the absence or the presence of IL-$1{\beta}$. The concentration of IL-6 produced form PDL cells was determined by enzym linked immunosorbent assay(ELISA). In unstimulated PDL cells, we detected constitutive production of IL-6 at 1st and 2nd day. IL-$1{\beta}$ increased IL-6 synthesis at 1st day and 2nd day. $17{\beta}$-estradiol had no significant effect on the secretion of this cytokine, either constitutively or after stimulation with IL- $1{\beta}$(0.05 ng/ml). 1,25-$(OH)_2D_3$($10^{-8}M$) decreased not only constitutive IL-6 production but also IL-$1{\beta}$-induced IL-6 production at 2nd day. These results suggest that 1,25-$(OH)_2D_3$ may control IL-$1{\beta}$-induced osteoclast differentiation by decreasing IL-$1{\beta}$-induced IL-6 secretion of PDL cells.

• Korean Journal of Microbiology
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• v.25 no.4
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• pp.339-345
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• 1987

A bacterium K-4-3, producing $\beta$-glucan hydrolyzing enzyme, was isolated from soil and identified to be Bacillus subtilis by its morpholohical and physiological characteristics. $\beta$-glucan was coloured using cibacron blue 3G-A and cross linded by the addition of 1, 4-butanedioldiglycidyl ether. This substrate was used for the isolation of $\beta$-glucanase producing microorganism. The $\beta$-glucan hydrolyzing enzyme actibity from isolated K-4-3 strain was also measured using the modified substrate. Bacillus subtilis K-4-3 produced the highest extracellular $\beta$-glucan hydrolyzing activity in the basal medium containing $\beta$-glucan as a carbon source, peptone and tryptone as a nitrogen source, and magnesium sulfate as an inorganic salt. The optimum temperature and initial pH for $\beta$-glucanase production by Bacillus subtilis K-4-3 were $37^{\circ}C$ and pH6. The highest enzyme activity was obtained at the culture age of 54 hrs with rotary shaking at $37^{\circ}C$. The crude enzyme showed the highest activity at pH 7.5-8.0 and $65^{\circ}C$.

• Korean Journal of Food Science and Technology
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• v.48 no.3
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• pp.296-300
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• 2016

The effect of different temperatures (45, 55, 65, and $75^{\circ}C$) on the extraction of ${\beta}$-glucan and the properties of extracted ${\beta}$-glucan were investigated with four different varieties of barley. Jeju naked barley, blue barley, beer barley, and black barley contained 6.85, 5.13, 3.58, and 4.16% of ${\beta}$-glucan, respectively. ${\beta}$-glucan in barley was extracted in the range of 64.88 to 93.84% depending on the extraction temperature and barley variety. The ${\beta}$-glucans in Jeju naked barley, Jeju blue barley, and black barley were optimally extracted at $65^{\circ}C$ for 3 h and Jeju beer barley at $75^{\circ}C$. The extracted ${\beta}$-glucan resolubilized to 43.48-81.73% and the ratio of ${\beta}(1{\rightarrow}3)$ to ${\beta}(1{\rightarrow}4)$ linkage was in the range of 1:3.8-5.8. These results suggest that purification and properties of ${\beta}$-glucan depend not only on the water extraction temperature, but also on the barley variety.

• Korean Journal of Pharmacognosy
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• v.31 no.1
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• pp.34-38
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• 2000

Three compounds were isolated from the roots of Astragalus membranaceus (Leguminosae). On the basis of spectroscopic evidences, the structures were characterized as $3-0-{\beta}-D-xylopyranosyl-(2',3'-O-diacetyl)-6-0-{\beta}-D-glucopyranosyl-3{\beta},6{\alpha},16{\beta},25-tetrahydroxy-20(R)$,24(S)-epoxy-cycloartane(Astragaloside I), $3-0-{\beta}-D-xylopyranosyl-(2'-O-acetyl)-6-0-{\beta}-D-glucopyranosyl-3{\beta},6{\alpha},16{\beta},25-tetrahydroxy-20(R)$,24(S)-epoxy-cycloartane(Astragaloside II), $3-0-{\beta}-D-xylopyranosyl-(2',4'-O-diacetyl)-6-0-{\beta}-D-glucopyranosyl-3{\beta},6{\alpha},16{\beta},25-tetrahydroxy-20(R)$,24(S)-epoxycycloartane(Isoastragaloside I). Full data of NMR including HMBC and 1D-TOCSY experiment of these compounds were reported for the first time.

• Applied Biological Chemistry
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• v.43 no.2
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• pp.136-140
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• 2000

Two steroidal saponins were isolated from MeOH extract of the rhizomes of Asparagus oligoclonos. Using the spectroscopic techniques of $^1H,\;^{13}C$ NMR and 2D NMR, they were identified as $3-O-[{\beta}-D-glucopyranosyl-(1{\rightarrow}2)-{\beta}-D-glucopyranosyl]-(25S)-spirostan-3{\beta}-ol$ and $3-O-{{\beta}-D-glucopyranosyl-(1{\rightarrow}2)-[{\beta}-D-xylopyranosyl-(1{\rightarrow}4)]-{\beta}-D-glucopyranosyl}-(25S)-spirostan-3{\beta}-ol$, respectively. They were first isolated from A. oligoclonos. The in vitro antibacterial activities as well as antibacterial spectrums against 20 bacteria strains were investigated with MIC test. Both saponins inhibited the growth of 10 bacteria strains at the concentration of$100\;{\mu}g/ml$.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.39 no.2
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• pp.121-127
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• 1994

A procedure for the direct detection of (1-3)-$\beta$-glucanase isozymes in electrophoresis gels was developed. The procedure employed the commercial preparation of AZCL-pachyman as a chromogenic substrate for (1-3)-$\beta$-glucanases. The procedure detected the three basic isozymes which have been known to be expressed in germinating barley kernels. A major acidic and a minor isozymes were also detected in germinating kernels. The procedure was proved to be fast, simple and sensitive enough to be used for the analysis of the expression of (1-3)-$\beta$-glucanase isozymes in plant tissues. The detection limit of the procedure for the commercial preparation of Penicillium (1-3)-$\beta$-glucanase was estimated to be as low as 50$\mu$U. The procedure could be used for the investigation of (1-3)-$\beta$-glucanases in laboratories facilitated with ordinary equipments and research personnel.