• Title/Summary/Keyword: KDA

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Effect of Phytate on the Electrophoretic Behavior of Rapeseed Protein Isolate (분리 유채단백의 전기영동 패턴에 미치는 Phytate의 영향)

  • Cho, Hee-Kyung;Yoon, Jae-Young;Lee, Su-Rae
    • 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.

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Effects on Mammalian Tissues and Cells by Sulfur Containing Compounds (황함유 화합물이 동물의 조직과 세포에 미치는 영향)

  • 이기섭;이정채;나상록;정희영;임계택
    • 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.

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CHARACTERISTICS OF THE SALIVARY PROTEINS IN THE CHILDREN WITH RAMPANT DENTAL CARIES (다발성 치아우식증 소아에서 타액 단백질의 특성)

  • Yang, Ho-Jeong;Chang, Hee-Soon;Lee, Sung-Ill;Choi, Byung-Jai
    • 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.

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' 97 KDA PHOTO

  • The Korean Dental Association
    • 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
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Quality Assurance Strategy for AGO Program in Korea (AGD(통합치과전문임상의)교육 프로그램 질 보장 방안)

  • Shin, Je-Won
    • 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.

Identification of two lectins containing the same sugar-specificity from Korean mistletoe

  • Kang, Tae-Bong;Yoo, Yung-Choon;Yoon, Seok-Min;Lee, Kwan-Hee;Kim, Jong-Bae
    • 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)

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Insulin induces nuclear translocation of insulin receptor and tyrosine phosphorylation of nuclear proteins in osteoblast (조골세포에서 인슐린 수용체의 세포핵으로의 이동과 타이로신 인산화)

  • Seol, Ki-Chun;Kim, Sung-Jin
    • 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.

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Enzymatic Properties of Fast-migrating Cationic Peroxidase Isozyme from Rice Callus

  • Yoo, Kyung-A;Lee, Mi-Young
    • 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.

Phosphorylation of the Nucleocapsid Protein of Bovine Coronavirus Expressed with a Recombinant Baculovirus Vector

  • Yoo, dongwan;Graham-J.Cox
    • Journal of Microbiology and Biotechnology
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    • v.2 no.2
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    • pp.122-128
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    • 1992
  • Post-translational modifications of the nucleocapsid protein of bovine coronavirus (Quebec strain) were investigated. Coronavirions were radiolabelled in vivo with inorganic $[^{32}P]$orthophosphate and analysed by SDS-PAGE, followed by autoradiography. A single polypeptide with a migration rate of 55 KDa was identified by metabolic phosphate labelling, demonstrating that the nucleocapsid protein of bovine coronavirus was a phosphoprotein. A gene encoding the nucleocapsid protein was inserted immediately downstream from the polyhedrin promoter of Autographa californica nuclear polyhedrosis baculovirus. Spodoptera frugiperda cells infected with this recombinant baculovirus synthesized a 55 KDa polypeptide, as demonstrated by immunoprecipitation with anti-nucleocapsid monoclonal antibody. The recombinant nucleocapsid protein synthesized in Spodoptera cells could also be labelled by $[^{32}P]$orthophosphate. Phosphoamino acid analysis showed that both serine and threonine residues were phosphorylated in authentic, as well as in recombinant nucleocapsid proteins, with a relative phosphorylation ratio of 7:3. Our studies demonstrated that the nucleocapsid protein of bovine coronavirus was a serine and threonine-phosphorylated protein and that Spodoptera insect cells were able to properly phosphorylate the relevant foreign proteins.

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