• Proceedings of the Korean Society of Soil and Groundwater Environment Conference
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• 2004.09a
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• pp.252-257
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• 2004

본 연구에서는 인산염을 이용여 납으로 오염된 Clay 사격장과 인위적으로 오염시킨 자연토양의 중금속의 고정화 실험을 수행하였다. 인산염 고정화제로는 DAP (diammonium phosphate)를 사용하였다. DAP를 투입한 중금속 오염토양을 고정화 실험과 TCLP로 용출 하였을 때, 99% 정도 고정화되었다. 인산염 투여양이 증가할수록 고정화 효율은 증가하는 것으로 나타났으며, 최적 인투입량은 128 mmol as P/kg인 것으로 나타났다. DAP 투입양이 증가할수록 토양의 pH는 증가하는 것으로 나타났으며, 토양의 초기 pH 변화에 따라 고정화 효율은 크게 변하지 않은 것으로 나타났으나, pH가 높을수록 고정화 효율은 작은폭으로 증가하는 것으로 나타났다.

• Journal of Life Science
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• v.13 no.6
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• pp.849-855
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• 2003

Nitric oxide (NO) plays an important role as a signaling molecule in the proliferation of placenta trophoblasts. In this study, we investigated the effect of NO on the activation of phospholipase C (PLC) in BeWo cells, choriocar-cinoma cell line. Sodium nitroprusside (SNP), an agent to produce NO spontaneously in cells, alone increased $［^3H］$ thymidine incorporation of BeWo cells, indicating NO stimulates proliferation of the cells. NO-induced proliferation of BeWo cells was blocked by U73122, an inhibitor of PLC, suggesting that NO-induced PLC activation is involved in the cell proliferation. NO also stimulated extracellular signal-regulated kinase (ERK) in BeWo cells, indicated by increased phosphorylation of ERK1/2 in Western blotting using anti-phospho-ERK1/2 antibody. NO-induced phos-phorylation of ERK1/2 was not abrogated by U73122. $PLC\gamma_1$l but not$PLC\gamma_2$ was tyrosine phosphorylated by SNP in immunoprecipitation assay using anti-$PLC\gamma_1$/$PLC\gamma_2$ antibodies, and SNP-induced phosphorylation of $PLC\gamma_1$ was abrogated by pre-treatment of cells with genistein and PD98059, indicating that NO induced-phosphorylation of $PLC\gamma_1$ is mediated by ERK. These results suggest that NO stimulates the proliferation of BeWo cells through ERK and $PLC\gamma_1$.

• Journal of the Korean Chemical Society
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• v.55 no.1
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• pp.86-91
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• 2011

Modified lignins were prepared. Soda and peroxy lignins were precipitated from black liquor produced from bagasse pulping with soda and peroxyacid pulping process. The precipitated lignins were hydrolyzed using 10% HCl. Different functional groups were also incorporated into lignin by carboxylation and phosphorylation reactions. Moreover crosslinking of these lignins were carried out using epichlorohydrin. Characterization of the modified lignins and lignins derivative were carried out using Infrared spectroscopy. Thermal analysis of these compounds were also carried out using TGA and DTA techniques. Efficiency of sorption of metal ions by the modified lignin was also investigated. It was found that, the peroxylignin and its derivatives show higher efficiency toward metal ions uptake than the soda lignin.

• Korean Journal of Soil Science and Fertilizer
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• v.37 no.1
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• pp.36-40
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• 2004

It is now widely accepted that immobilized microbial cells can overcome some of the problems associated with microbial survival stability, efficacy, storage, transportation and ease of application in agricultural environments. Pantoea agglomerans, a phosphate solubilizing bacterium, was immobilized in alginate, agar and gelatin carriers. All the three immobilfized carriers with bacterial cells of P. agglomerans were compared for solubilization of tricalcium phosphate in pure liquid cultures. While alginate beads were tested for phosphate solubilization on alternate days up to five days, agar beads and gelatin cubes were subjected for one time phosphate solubilization analysis after seven days. Both alginate and agar immobilized cells of P. agglomerans exhibited higher efficiency in increasing the solubilizaliun of tricalcium phosphate than gelatin immobilized cells. The culture filtrate of alginate bead inoculation treatment registered a rapid increase in soluble phosphate concentration upon incubation. A corresponding decrease in the pH of the medium was also observed in all the treatments.

• Korean Journal of Soil Science and Fertilizer
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• v.38 no.4
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• pp.188-193
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• 2005

Pantoea agglomerans immobilized in alginate solubilized four different rock phosphates efficiently under in vitro conditions. The solubilization pattern differed according to the rock phosphate source, where maximum solubilization of Morocco and Tunisia rock phosphates (215.6 and $186.1mg\;P\;L^{-1}$) on 6 days, Israel rock phosphate ($60.98mg\;P\;L^{-1}$) and tricalcium phosphate ($132.3mg\;P\;L^{-1}$) on 10 days and China rock phosphate ($48.8mg\;P\;L^{-1}$) on 12 days after inoculation was observed. The shelf life of the immobilized bacteria immobilized beads stored in two different temperatures was studied for six months. Beads stored at both room temperature as well as cold storage ($4^{\circ}C$) were found equally good in supporting the bacterial population as well as phosphate solubilizing activity. P. agglomerans immobilized in alginate might be exploited for large scale biosolubilization of rock phosphates intended for fertilizer use.

• Journal of the Korean Chemical Society
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• v.31 no.1
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• pp.84-93
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• 1987

The study was done with a focus on making the optimum condition on phosphorylation of deoxyribonucleoside with o-chlorophenylphosphoroditriazole as a phosphorylating agent. The result showed that the addition of 5 volume % pyridine to the dioxane solution accelerated the rate of reaction to a great extent and turned out to nearly quantitative yields on phosphorylation. On the basis of this improvement of optimum reaction conditions, a more efficient method to synthesize all-protected dideoxyribonucleotide from N, 5-O-blocked deoxyribonucleoside was developed. The dodecamer with a Hind Ⅲ recognition site was readily synthesized from five different dimers which were prepared through the newly improved method.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2001.05a
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• pp.114-115
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• 2001

Alloxan은 glucokinase효소가 기질인 glucose결합부위인 -SH기를 경쟁적으로 저해함으로서 glucose의 초기 인산화를 억제하여 당뇨병을 유도시키는 화학물질이다. 본 연구에서는 이제까지의 조직학적이고 혈청학적인 연구에서 한 단계 나아가 효소학적인 측면에서 당대사와 인슐린 분비 조절인자로 알려진 glucokinase와 혈중 당을 조직내로 흡수하여 인산화시키는 효소인 hexokinase에 대한 다시마 열수추출물의 효과를 분석 검토하였다. (중략)

• Journal of Life Science
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• v.26 no.7
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• pp.868-874
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• 2016

Receptor-interacting protein kinase 1 (RIPK1) and RIPK3 are members of the serine or threonine protein kinase superfamily that phosphorylates the hydroxyl group of serine or threonine through the highly conserved kinase region. The RIPK family plays a crucial role not only in inflammation and innate immunity, but also in mediating programmed cell death, such as apoptosis and necroptosis. The interaction between RIPK1 and other TNFR1-related proteins has been shown to assemble a signaling complex I that controls activation of the pro-survival transcription factor NF-κB upon binding of cytokines to TNF receptor 1 (TNFR1). Moreover, RIPK1 and RIPK3 interact through their RIP homotypic interaction motifs (RHIMs) to mediate programmed necrosis, which has long been considered an accidental and uncontrolled cell death form with morphological characteristics differing from those of apoptosis. Highly conserved sequences of RHIM in RIPK1 and RIPK3 were shown to regulate their binary interaction, leading to assembly of a cytosolic amyloid complex termed the “necrosome”. The necrosome also contains mixed lineage kinase domain-like protein (MLKL), which has been found recently to be a substrate of RIPK3 to mediate downstream signaling. This review provides an overview of the functional and physiological characteristics of RIPKs and MLKL in TNF signaling.

• Journal of Life Science
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• v.23 no.2
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• pp.324-331
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• 2013

The addition and removal of N-acetylglucosamine (GlcNAc) molecules on serine or threonine residues of a protein is called O-GlcNAcylation. This post-translational modification occurs on both cytoplasmic and nuclear protein, and is fast and reversible as comparable to phosphorylation. In contrast to the phospho-signaling cycles, this emerging moon-lightening signaling is cycled by only two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). The simple machinery is a good evolutionary adaptation of a cell for quick accommodation to continuously fluctuating intra- and extracellular microenvironments. Rather than "switching" on or off a specific proteins - this would be done by phosphorylation where numerous specific kinases and phosphatases are involved - O-GlcNAcylation would play a "rheostat" which would be much more delicately increase or decrease the efficacy of signal transductions in response to cellular nutrient and stress conditions. Interestingly, recent evidence indicates that O-GlcNAc is further modified by phosphorylation. The O-GlcNAc-P will upgrade the modulation efficiency of cellular processes to continuous 'analogue' level. So far, only one protein AP180 was reported to have O-GlcNAc-P on Thr310. But, proteomic data from our laboratory indicate that there are multiple O-GlcNAc-P proteins, constituting "O-GlcNAc-P'om". This will focus on the possibility of existence of "O-GlcNAc-P'om".

• Korean journal of food and cookery science
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• v.10 no.2
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• pp.161-165
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• 1994

It was aimed to investigate the effects of caffeic acid on the rates of Maillard reaction. The rates of browning reaction increased as the browning temperature increased. The color intensity of the browning mixtures indicated to depend on the amino acid rather than reducing sugar. Also, the color intensity of the browning mixtures increased more rapidly in the presence of caffeic acid. The increase in color intensity seemed to depend mainly to the polymerization of o-quinones formed from caffeic acid. The caffeic acid, furthermore, appeared to enhance the color intensity of the browning mixtures through the interaction with amino acid, especially methionine and phenylalanine. The activation ener-gies of the browning reaction without caffeic acid were 108∼130 J/mol, and Q10 values were 2.6∼3.2. The activation energies and Q10 values of browning mixtures decreased in the presence of CA. The activation energies of the browning mixtures with caffeic acid were 90∼101J/mol, and Q$\_$10/ values were 2.0∼2.6.