• Journal of Life Science
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• v.5 no.4
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• pp.170-180
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• 1995

A carotennnoprotein from the skin of Ascidian(Halocynthia roretzi) was extracted by Triton X-100 and purified by ammonium sulfate fraction, SephadexG-200 charomatography and DEAE-cellulose ion exchange chromatography. The carotenoprotein was redwith broad $\lambda$$_{max}$ between 495, 467 and 318nm. The red carotenoprotein had an approximate molecular weight of 326KDa(gel filtration). SDS-PAGE indicated the presence of two polypeptodes of 84.1KDa and 74.4KDa, with different mobility in polyacrylamide gel electrophoresis. In the presence of denaturing agents such as organic solvent aand extreme pH, the red complex readily disociates to liberate the yellow carotenoid($\lambda$$_{max}$ 452nm) and a colourless apoprotein. The amino acid composition of carotenoprotein were mainly threonine(15.2%), aspartic acid(12.2%), glutamic acid(11.9%) and serine(9.6%), while proline was not found. The carotenoprotein consisted of lipids as structure units. Its major fatty acids composion were C$_{18:1}$, C$_{16:1}$, and C$_{16:0}$. The monounsaturated fatty acids(41.5%) contained abundant content compared to other fatty aacids(polyunsaturated fatty acids 37.4%, saturated fatty acids 20.6%).

• Korean Journal of Food Science and Technology
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• v.24 no.3
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• pp.284-288
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• 1992

This study was undertaken to investigate the effect of pH and phytate level on the solubility of the protein due to binding between phytate and low-phytate rapeseed protein isolate by means of SDS-polyacrylamide gel electrophoresis. Results showed that the number of protein bands decreased by the increasing amount of phytate added to the soluble extract at pH 2.0 and 5.0 whereas there was no change at pH 11.5. Among 18 bands of rapeseed proteins at pH 2.0, seven bands (105.8, 52.3, 37.3, 34.8, 26.3, 21.3, 18.4 KDa) were removed by precipitation with 100 mg phytate addition and six bands (78.8, 46.5, 19.4, 16.8, 11.7, 8.5 KDa) further disappeared by 150 mg phytate addition. Among 15 bands at pH 5.0, only four bands disappeared by phytate addition. It is suggested that the functionality of rapeseed protein isolate can be improved by lowering the phytate content.

• Toxicological Research
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• v.15 no.1
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• pp.79-87
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• 1999

To know the stress response and antioxidative effect of sulfur containing compounds, we observed the expression of the stress protein (heat shock protein; inducible protein) from mouse tissues and evaluated the protective effects to hydroxyl radical in mouse brain cell culture. Cysteine, methionine or sodium sulfide was fed by oral administration of 1 ml/per 6hr/three times with 1 mM, 2mM or 3mM to mouse, respectively. After that, the stress proteins were extracted from mouse tissues and analyzed the features of expression. The stress proteins by sulfur containing compounds were showed different aspects in the kinds and concentrations of their compounds, and in the tissues of mouse. In the liver, the stress proteins were appeared at different time on the concentration of sulfur containing compounds and had less than 20 KDa as small molecules. In general, the molecular weights of stress protein in liver, the stress proteins were appeared at different time on the concentration of sulfur containing compounds and had less than 20 KDa as small molecules. In general, the molecular weights of stress protein in the spleen were evaluated from 32KDa to 50KDA, and the induced times were relatively late at high concentration of cysteine, early at low concentration of methionine or sodium sulfide. The stress proteins in mouse muscle were detected mostly between 24hr after treatment of sulfur containing compounds. Their molecular weights were 15~24KDa. In the antioxidative effects of sulfur containing compounds to hydroxyl radical, cell viabilities were measured by 63.2% at 10 $\mu\textrm{M}$, 65.5% at 50 $\mu\textrm{M}$, 68.6% at 100 $\mu\textrm{M}$, 78.3% at 150 $\mu\textrm{M}$, or 83.0% at 200 $\mu\textrm{M}$ of cysteine, respectively. At addition of methionine, the cell viabilities were assessed as 58.1% at 10 $\mu\textrm{M}$, 62.8% at 50 $\mu\textrm{M}$, 75.7% at 100 $\mu\textrm{M}$, 78.6% at 150 $\mu\textrm{M}$, and 79.2% at 200 $\mu\textrm{M}$ after 4hrs exposure with 20mU/ml glucose oxidase (GO) system, while the numbers of live cells to hydroxyl radicals in treatment of sodium sulfide were showed 48.6% at 10 $\mu\textrm{M}$, 54.8% at 100 $\mu\textrm{M}$, 51.8% at 150 $\mu\textrm{M}$, and 51.6% at 200 $\mu\textrm{M}$ in the neuronal cells. In the inhibitory effects on the proliferation of tumor cells, percentages of dead cells of the CT-26 or HeLa cell were generally less than 30% even 48hr after addition of sulfur containing compounds. Conclusively, the results of these experiments indicate that stress protein by sulfur containing compounds can be used as physiological indicator for animal nutrition and for environment, and also that cysteine and methionine can play critical roles as an antioxidant.

• Journal of the korean academy of Pediatric Dentistry
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• v.23 no.2
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• pp.415-427
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• 1996

As a part of host factors of dental caries, saliva has been well known for its important role in relation to dental caries. The studies on its physical and chemical characteristics on development and progress of dental caries has been conducted. Recently, various comparisons between saliva of caries-susceptable individuals and caries-free individuals has been done and the efforts to understand the mechanisms of salivary intervention of development and progress of dental caries is actively in progress. In this study, 15 children with rampant dental caries and 15 caries free children without any systemic diseases from the ages of 2 to 5 were chosen for the experiment and the whole saliva and parotid saliva from each individuals were collected and protein compositions were compared using polyacrylamide gel electrophoresis (PAGE). As results of this study, in parotid saliva, there was no difference in protein compositions between the rampant dental caries and the caries free children. While electrophoresis was done with the whole saliva, protein with 120 KDa was found in children with rampant dental caries. However, this protein was not found or unclear, if any for the caries free group. (Exceptionally, clear protein band was present for one person.) Protein compositions of whole saliva of rampant dental caries group was compared before and after the caries control and thick and clear protein bands of about 120 KDa were found in both cases. Protein compostions of caries free children and adults were identical. Quantitative analysis of protein was done for the rampant dental caries group and the control group and no significant difference was found. Taken all together, protein with molecular weight of 120 KDa, found in rampant dental caries group, was still present when the treatment for the dental caries was done so it can be assumed that this protein has no interrelation with the presence of active carious lesions during saliva collecting. It can also be presumed that this specific salivary protein with the molecular weight of 120 KDa found in rampant dental caries group has effect on development and progress of dental caries. Identification on this protein with the molecular-weight of 120 KDa and the role of this protein against dental caries remain to be solved.

• The Journal of the Korean dental association
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• v.39 no.5 s.384
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• pp.384-385
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• 2001

• The Journal of the Korean dental association
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• v.35 no.12 s.343
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• pp.921-925
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• 1997

• The Journal of the Korean dental association
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• v.48 no.11
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• pp.790-796
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• 2010

Currently, KDA adopted new post-graduated program; advanced education general dentistry(AGD) for 3 years preparation. The AGO program provides the resident the opportunity to deliver the highest quality of comprehensive dental care to the broadest range of the population with a knowledge, comfort, and ease in treating the high risk patient. The purpose of this article is to study the assurance systems of AGO programs in USA and Japan and to suggest a piece of advice whether we choose the way of AGO program assurance system in Korea.

• Proceedings of the PSK Conference
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• 2003.04a
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• pp.213.2-214
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• 2003

Three mistletoe lectins (ML -I, ML -IIU, ML -IIL) have been identified in Europe based on sugar specificities for galactose(Gal) and N-acetyl galactosamine(GalNAc). Korean mistletoe lectins have been known as mainly ML -II type. In previous results, we suggested that there are two lectins, 64 KDa and 60 KDa, in Korean mistletoe lectin (KML -C). (omitted)

• Proceedings of the Korean Society of Applied Pharmacology
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• 2001.11a
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• pp.101-101
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• 2001

In the present study, we explored to determine if insulin has any effect on the nuclear translocation of insulin receptor and tyrosine phosphoryaltion of nuclear proteins in the UMR-106 cells. Significant amount of insulin receptors and IRS-1 proteins were detected in the nucleus. IRS-1 and PI$_3$-Kinase appeared to translocate to the nucleus in a time dependent manner. Tyrosine phosphorylation of a number of proteins including 180 KDa, 85 KDa protein in the nucleus was significantly stimulated by insulin, suggesting IRS-1 and PI$_3$-Klnase was activated in the nucleus by insulin treatment. In addition, p70 S6 Kinase, a downstream target of PI3-Kinase was transiently appeared in the nucleus by insulin and its activity was stimulated by insulin. These results suggest that the insulin signaling system containing insulin receptor, IRS-1, PI$_3$-Kinase and p70 S6 Kinase operates in the nucleus of osteoblast cells. The nuclear insulin-mediated tyrosine phosphorylation may play an essential role in the gene expression, differentiation and growth of osteoblast cells.

• Journal of Plant Biotechnology
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• v.4 no.1
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• pp.39-44
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• 2002

The fast-migrating cationic peroxidase isozyme, named RC3, was purified from rice (Oryza sativa cv. Nak-Dong) callus. Purification of the enzyme was accomplished by ammonium sulfate fractionation, CM-cellulose ionexchange chromatography, and Sephacryl S-100 gel filtration. The molecular mass of the enzyme was about 34 KDa as determined by SDS-PACE and 38 KDa by Sephacryl-100 gel filtration. The pI value of the enzyme was 8.9. Antiserum against RC3 was raised in rabbits, and anti RC3 antiserum reacted with RC3 isozyme by Ouchterlony double immunodiffusion. The optimum pHs and Km values of the enzyme for various substrates were determined. Kinetic studies with various substrates showed that RC3 had very low Km value of 0.01 mM for ferulic acid and ascorbic acid. However, the enzyme did not use esculetin as a substrate.