• Title/Summary/Keyword: Protein A

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Effects of Overexpression of C5 Protein on rnpB Gene Expression in Escherichia coli

  • Kim, Yool;Lee, Young-Hoon
    • Bulletin of the Korean Chemical Society
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    • v.30 no.4
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    • pp.791-793
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    • 2009
  • Escherichia coli RNase P is composed of a large RNA subunit (M1 RNA) and a small protein subunit (C5 protein). Since both subunits are assembled in a 1:1 ratio, expression of M1 RNA and C5 protein should be coordinately regulated for RNase P to be efficiently synthesized in the cell. However, it is not known yet how the coordination occurs. In this study, we investigated how overexpression of C5 protein affects expression of the rnpB gene encoding M1 RNA, using a lysogenic strain, which carries an rnpB-lacZ transcription fusion. Primer extension analysis of rnpB-lacZ fusion transcripts showed that the overexpression of C5 protein increased the amount of the fusion transcripts, suggesting that rnpB expression increases with the increase of intracellular level of C5 protein.

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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Mapping protein interaction computatonally

  • Park, Jong-H.
    • Proceedings of the Korean Society for Bioinformatics Conference
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    • 2000.11a
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    • pp.23-27
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    • 2000
  • Protein interaction is an important research topic in Bioinformatics. A novel computational method of protein interaction was developed. It shows the diverse pattern of protein protein interaction,

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Characterization of Protein Kinases Activated during Treatment of Cells with Okadaic Acid

  • Bogoyevitch, Marie A.;Thien, Marilyn;Ng, Dominic C.H.
    • BMB Reports
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    • v.34 no.6
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    • pp.517-525
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    • 2001
  • Six renaturable protein kinases that utilize the myelin basic protein (MBP) as a substrate were activated during prolonged exposure of cardiac myocytes to okadaic acid (OA). We characterized the substrate preference and activation of these kinases, with particular emphasis on 3 novel kinases-MBPK-55, MBPK-62 and MBPK-87. The transcription factors c-Jun, Elk, ATF2, and c-Fos that are used to assess mitogen-activated protein kinase activation were all poor substrates for these three kinases. MAPKAPK2 was also not phosphorylated. In contrast, Histone IIIS was phosphorylated by MBPK-55 and MBPK-62. These protein kinases were activated in cultured cardiac fibroblasts, H9c2 cardiac myoblasts, and Cos cells. High concentrations (0.5 to $1\;{\mu}M$) of OA were essential for the activation of the protein kinases in all of the cell types examined, whereas calyculin A [an inhibitor of protein phosphatase 1 (PP1) and PP2A], cyclosporin A (a PP2B inhibitor), and an inactive OA analog all failed to activate these kinases. The high dose of okadaic acid that is required for kinase activation was also required for phosphatase inhibition, as assessed by immunoblotting whole cell lysates with anti-phosphothreonine antibodies. A variety of chemical inhibitors, including PD98059 (MEK-specific), genistein (tyrosine kinase-specific) and Bisindolylmaleimide I (protein kinase C-specific), failed to inhibit the OA activation of these kinases. Thus, MBPK-55 and MBPK-62 are also Histone IIIS kinases that are widely expressed and specifically activated upon exposure to high OA concentrations.

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Cucumber Mosaic Virus 1a Protein Interacts with the Tobacco SHE1 Transcription Factor and Partitions between the Nucleus and the Tonoplast Membrane

  • Yoon, Ju-Yeon;Palukaitis, Peter
    • The Plant Pathology Journal
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    • v.37 no.2
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    • pp.182-193
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    • 2021
  • The transcription factor SHE1 was identified as an interacting partner with the cucumber mosaic virus (CMV) 1a protein in the yeast two-hybrid system, by a pull-down assay, and via bimolecular fluorescent complementation. Using fluorescent-tagged proteins and confocal microscopy, the CMV 1a protein itself was found distributed predominantly between the nucleus and the tonoplast membrane, although it was also found in speckles in the cytoplasm. The SHE1 protein was localized in the nucleus, but in the presence of the CMV 1a protein was partitioned between the nucleus and the tonoplast membrane. SHE1 expression was induced by infection of tobacco with four tested viruses: CMV, tobacco mosaic virus, potato virus X and potato virus Y. Transgenic tobacco expressing the CMV 1a protein showed constitutive expression of SHE1, indicating that the CMV 1a protein may be responsible for its induction. However, previously, such plants also were shown to have less resistance to local and systemic movement of tobacco mosaic virus (TMV) expressing the green fluorescent protein, suggesting that the CMV 1a protein may act to prevent the function of the SHE1 protein. SHE1 is a member of the AP2/ERF class of transcription factors and is conserved in sequence in several Nicotiana species, although two clades of SHE1 could be discerned, including both different Nicotiana species and cultivars of tobacco, varying by the presence of particular insertions or deletions.

The Effect of Serum Cholesterol Levels of Experimntal Rats fed by Vit. E, Garlic and different the Levels of Proteins in their Diet (백서(白鼠)에 있어서 식이배합(食餌配合)이 혈액내(血液內) Cholesterol에 미치는 영향)

  • Kim, E-Sik
    • Journal of Nutrition and Health
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    • v.7 no.1
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    • pp.45-50
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    • 1974
  • Biochemical studies such as growth rate, blood cholesterol and ascorbic acid contents in various organs of albino male rats were studied in the Garlic, Vitamin E, high and low protein diet fed groups. The results of this study were summarized as follows : 1) Either single 10% or 30% protein diet fed rats were not shown growth rate properly. In supplementation of Vitamin E or Garlic on 30% protein growth rate was a more increased than that of the 10% protein diet group. 2) The rate of food consumption of rats fed a 10% or 30% protein diet supplemented with Vitamin E and Garlic was more increased than that of the control Group receving 10% or 30% protein diet alone. 3) No essential difference was observed between the cholesterol level in blood of rats fed 10% protein diet supplemented with Vitamin E and Garlic and that of rats Receiving 10% protein diet alone. But the cholesterol level in blood of rats fed 30% protein diet supplemented with Vitamin E and Garlic was lower than that of control receiving 30% protein diet alone. 4) The Vitamin C contents in various organs of rats fed the diet supplemented with Vitamin E and Garlic seems to be a little higher than that of the control group fed the protein diet alone.

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Hereditary protein S deficiency presenting acute pulmonary embolism

  • Kim, Jiwan;Kim, Sung Hea;Jung, Sang Man;Park, Sooyoun;Yu, HyungMin;An, Sanghee;Kang, Seonghui;Kim, Hyun-Joong
    • Journal of Yeungnam Medical Science
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    • v.31 no.1
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    • pp.52-55
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    • 2014
  • Protein S deficiency is one of the several risk factors for thrombophilia and can cause blood clotting disorders such as deep vein thrombosis and pulmonary embolism. A 54-year-old man was admitted with the complaint of dyspnea and was diagnosed with pulmonary embolism. The patient had very low level of free protein S, total protein S antigen, and protein S activity (type I protein S deficiency). In history taking, we found that his mother, 78 year old, had a history of same disease 10 years ago, and confirmed the pronounced low level of protein S. The patient's son also had very low level of protein S, however there had not been any history of pulmonary embolism yet. This case study suggests that asymptomatic persons with a family history of protein S deficiency and pulmonary embolism should be checked regularly for early detection of the disease, as protein S deficiency can be suspected.

THE INFLUENCE OF DIETARY PROTEIN AND ENERGY LEVELS ON EGG QUALITY IN STARCROSS LAYERS

  • Uddin, M. Salah;Tareque, A.M.M.;Howlider, M.A.R.;Khan, M. Jasimuddin
    • Asian-Australasian Journal of Animal Sciences
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    • v.4 no.4
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    • pp.399-405
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    • 1991
  • The interaction of 4 dietary crude protein (13, 16, 19 or 22%) and 4 metabolizable energy (2600, 2800, 3000 or 3100 kcal ME/kg) levels on egg quality performances of Starcross layers were assessed between 245 and 275 days of age. The egg weight increased significantly with the increasing dietary protein and energy levels. But egg shape index, albumen index, yolk index, yolk dry matter, yolk protein, yolk fat, albumen protein and shell tickness were similar at all dietary protein and/or energy levels. The egg specific gravity and albumen weight increased but the yolk, weight, Haugh unit and albumen drymatter decreased with the increase of dietary protein levels and showed irregular trend with energy levels. The albumen dry matter and egg shell weight, however, were not affected by energy and protein levels. Simultaneous increase of protein and energy increased specific gravity, albumen index and shell thickness at a greater rate than that increased by the increase of protein or energy alone.

The Effect of the Difference Between Natural Protein and Whey Protein Intake During the 12 weeks of Resistance Training Exercise on Changes in Solt Lean Mass and Body Composltion (12주저항트레이닝 운동시 천연단백질과 분리유청단백질 섭취의 차이가 근육량 및 신체구성에 미치는 영향)

  • PARK, Won-Deok
    • Journal of Fisheries and Marine Sciences Education
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    • v.28 no.5
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    • pp.1220-1230
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    • 2016
  • The purpose of this study is to investigate the effect of 20s university student bodybuilders' protein intake differences with resistant exercise(weight training) by 12 weeks on solt lean mass and body composltion. Natural protein(Chicken breast meat) intake group and Whey protein isolates(WPI) intake group are the experimental groups. Conventional meal intake group is the control group. This study proposes a efficient protein diet for weight training. The results were as follows. In the experimental group(natural protein intake), muscle mass and lean body mass was significantly increased, but body fat percentage was significantly decreased. In the experimental group(WPI intake), muscle mass and lean body mass was significantly increased, but body fat percentage was significantly decreased. In the control group(conventional meal intake), muscle mass and lean body mass was insignificantly increased, but body fat percentage was insignificantly decreased. In addition, there was not a significant difference among intake groups, and also not a differentiated effect between natural protein and WPI intake. In conclusion, natural protein and WPI made muscle mass and lean body mass rise, body fat percentage reduced effectively. Only WPI intake(without natural protein intake) was the efficient mean to increase muscle mass and lean body mass, and to decrease body fat percentage.

Increase in dietary protein content exacerbates colonic inflammation and tumorigenesis in azoxymethane-induced mouse colon carcinogenesis

  • Tak, Ka-Hee;Ahn, Eunyeong;Kim, Eunjung
    • Nutrition Research and Practice
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    • v.11 no.4
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    • pp.281-289
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    • 2017
  • BACKGROUND/OBJECTIVE: The incidence of colorectal cancer (CRC) has been attributed to higher intake of fat and protein. However, reports on the relationship between protein intake and CRC are inconsistent, possibly due to the complexity of diet composition. In this study, we addressed a question whether alteration of protein intake is independently associated with colonic inflammation and colon carcinogenesis. MATERIALS/METHODS: Balb/c mice were randomly divided into 4 experimental groups: 20% protein (control, 20P, 20% casein/kg diet), 10% protein (10P, 10% casein/kg diet), 30% protein (30P, 30% casein/kg diet), and 50% protein (50P, 50% casein/kg diet) diet groups and were subjected to azoxymethane-dextran sodium sulfate induced colon carcinogenesis. RESULTS: As the protein content of the diet increased, clinical signs of colitis including loss of body weight, rectal bleeding, change in stool consistency, and shortening of the colon were worsened. This was associated with a significant decrease in the survival rate of the mice, an increase in proinflammatory protein expression in the colon, and an increase in mucosal cell proliferation. Further, colon tumor multiplicity was dramatically increased in the 30P (318%) and 50P (438%) groups compared with the control (20P) group. CONCLUSIONS: These results suggest that a high protein diet stimulates colon tumor formation by increasing colonic inflammation and proliferation.