• Title/Summary/Keyword: 30K protein

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Purification and Characterization of Protein Carboxyl O-Methyltransferase from Porcine Spleen

  • Yoon, Sung-Pil;Son, Min-Sik;Han, Jeung-Whan;Lee, Hyang-Woo;Hong, Sung-Youl
    • BMB Reports
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    • v.30 no.6
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    • pp.410-414
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    • 1997
  • We purified a protein carboxyl O-methyltransferase (protein methylase II) from porcine spleen to homogeneity. The molecular weight of the porcine spleen protein methylase II (ps-PM II) was estimated to be 27,500 daltons on SDS-PAGE. Amino acid sequence of N-terminal 28 residues for ps-PM II was identified. Amino-terminal three amino acid residues of ps-PM II were deleted when compared to those of other protein carboxyl methytransferase. S-Adenosyl-L-homocysteine competitively inhibits ps-PM II with a K, value of $1.63{\times}10^{-7}M$. Myelin basic protein exhibited the highest methyl-accepting capacity among the proteins tested.

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Effects of Heavy Metals on Growth and Protein Synthesis in Cyanobacterium synechocystis sp. PCC 6803 (중금속이 Cyanobacterium synechocystis sp.PCC 6803의 성장과 단백질 합성에 미치는 영향)

  • 강경미;장남기
    • Asian Journal of Turfgrass Science
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    • v.10 no.4
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    • pp.315-329
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    • 1996
  • The changes of growth and protein synthesis pattern by aluminum (Al), cadmium (Cd), zinc (Zn) treatments were studied in Cyanobacterium synechocystis sp. PCC 6803. When exposed to Al from 5ppm to 3oppm, synechocystis grows normally. But more than that retard the growth of algae notably. The 0.05ppm Cd additions had no effect on the growth of algae. 0.1, 0.2, and 0.5ppm Cd inhibited growth. Under 1 and 2ppm Cd stress, growth was greatly diminished. Zn had dual effects. The growth of algae in media containing 5ppm was stimulated. As concentration increases more than l5ppm, growth inbition increases. Under 25ppm Zn stress, growth was greatly diminished. According to logistic theory, r and K values of each heavy metal-treated groups were estimated. Correlation analysis of r and K values with metal concentration shows that there is negative correlation between K and concentration in Cd and Zn treatments. Critical concentration which shows lethal or sublethal effect was estimated by t-test of each r and K value. The cells cultured in 10, 20, 30, 40 and 5oppm of Al, 1 and 2ppm of Cd, and 10, 15, 20, 25 and 30ppm of Zn for 4 days was used for protein analysis. Analysis of protein synthesis with SDS-PACE showed alterations of protein synthesis pattern. The synthesis of protein about 220kD increased markedly. In this study, it showed that resistance mechanism against Al, Cd, and Zn is K selection and that metal stress induced the change of protein synthesis in Cyanobacterium synechocystis sp. PCC 6803.Key words:Cyanobacterium synechocystis sp. FCC 6803, Heavy metals, Aluminum, Cadmiutm Zinc, Crowth, Frotein synthesis.

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The Effect of NaCI Treatment on the Freezing Tolerance and Protein Patterns of Carrot Callus Suspension Culture

  • Moon, Soon-Ok;Park, Sook-Hee;Cho, Bong-Heuy
    • BMB Reports
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    • v.30 no.1
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    • pp.21-25
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    • 1997
  • The growth. freezing resistance and electrophoretic protein patterns of carrot callus cultures were investigated following treatment with NaCl for various' intervals at 20$^{\circ}C$. Following 7 day exposure to 250 mM NaCl. freezing tolerance increased, which was measured by 2.3.5-triphenyl tetrazolium chloride (TTC) assay and fresh weight was reduced compared to control cells. Changes of electrophoretic patterns of total and boiling stable proteins were investigated using one or two dimensional gel system. Several proteins with molecular weight of 43 and 21 kDa increased by NaCl treatment. The most prominent change was detected in 21 kDa protein. The steady state level of this protein increased in NaCl treated cells, but decreased in control cells. Twenty one kDa protein was detected only in the NaCl treated cell when boiling stable protein was analyzed. The isoelectric point of 21 kDa protein was identified as 5.7. The timing of increase of 21 kDa protein was correlated to freezing resistance which implied the role of this protein in the induction of freezing resistance of the cell.

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Pathogenicity and localization of the tobacco mosaic virus 4.8 kDa protein(oral)

  • Palukaitis, P.;Canto, T.;MacFarlane Scottish, S.A.
    • Proceedings of the Korean Society of Plant Pathology Conference
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    • 2003.10a
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    • pp.65.1-65
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    • 2003
  • In addition to the five well-characterized genes of Tobacco mosaic virus (TMV), this virus contains a sixth open reading frame (ORF6) that encodes a 4.8 kDa protein. TMV ORF6 overlaps the ORFs encoding the 30 kDa movement protein and the adjacent 17.5 kDa capsid protein. Although the 4.8 kDa protein could not be detected in vivo, alteration of the AUG codons of this ORF resulted in a mutant virus that attenuated the virulence of the mutated TMV in Nicotiana benthamiana, but not N. tabacum (tobacco). These sequence changes did not affect either the replication or movement of the mutated TMV. Expression of TMV ORF6 from the virus expression vector Potato virus X (PVX) intensified the virulence of this virus in N. benthmiana, but not tobacco, while expression of TMV ORF6 from the virus expression vector Tobacco rattle virus enhanced the pathogenicity observed in both N. benthamima and tobacco. Thus, the TMV ORF6 is a host- and virus-specific. virulence factor. However, two separate assays indicated that the TMV 4.8 kDa protein was not a suppression of RNA silencing. A fusion protein formed between the TMV 4.8 kDa protein and the green fluorescent protein was expressed from the PVX vector and localized to plasmodesmata. Possible roles of the 4.8 kDa protein in pathogenicity will be discussed

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Regulatory Role of the Serpin Strain

  • Seo, Eun-Joo;Yu, Myeong-Hee
    • Proceedings of the Korean Biophysical Society Conference
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    • 2002.06b
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    • pp.30-30
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    • 2002
  • The native forms of common globular proteins are in their most stable state but the native forms of plasma serpins (serine protease inhibitors) show high-energy state interactions. The high-energy state strain of a ${\alpha}$$_1$-antitrypsin, a prototype serpin, is distributed throughout the whole molecule, but the strain that regulates the function directly appears to be localized in the region where the reactive site loop is inserted during complex formation with a target protease.(omitted)

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Fish Meal Replacement by Cottonseed and Soybean Meal in Diets for Juvenile Olive Flounder, Paralichthys olivaceus

  • Pham, Minh-Anh;Lee, Kyeong-Jun;Lim, Se-Jin;Lee, Bong-Joo;Kim, Sung-Sam;Park, Young-Jun;Lee, Sang-Min
    • Journal of Aquaculture
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    • v.18 no.3
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    • pp.215-221
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    • 2005
  • This study was conducted to investigate the effects of dietary supplementation of cottonseed and soybean meal on growth performance of juvenile olive flounder (Paralichthys olivaceus). Nine hundred fish $(0.74{\pm}0.11g)$ in the early juvenile stage were randomly divided into 15 groups, and 3 groups were fed one of five isonitrogenous (56% CP) and isocaloric $(16.3\;MJ\;kg^{-1})$ diets replacing 0, 10, 20, 30, and 40% of fish meal protein by equal proportion (1:1, w:w) of cottonseed and soybean meal (CS) (designated by Control, CS10, CS20, CS30, and CS40, respectively). A solvent extracted cottonseed meal containing high crude protein (44%) and low fiber content (<12%) was used in this study. After 10 weeks of feeding trial, the growth offish fed diets CS10, CS20, and CS30 were not significantly (P>0.05) different compared to that of fish fed the control diet. However, diet CS40 exhibited significantly lower (P<0.05) growth performance than the control diet. No differences were observed in whole body composition of fish fed all the experimental diets. This study indicates that mixture of cottonseed and soybean meal with lysine and methionine supplementation can replace up to 30% fish meal protein in diet for olive founder at the early juvenile stage. However, we suggest that 20% of fish meal protein replacement by cottonseed (10%) and soybean (10%) meal can be the optimum level for commercial use in safety according to the growth performances.

Evaluation of a Newly Developed Fish Meal Analogue (BAIFA-M) in Immature Korean Rockfish, Sebastes schlegeli, Reared in Cage Culture System

  • Kim, Kang-Woong;Choi, Jae-Young;Sungchul C. Bai
    • Journal of Aquaculture
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    • v.13 no.3
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    • pp.259-265
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    • 2000
  • Four experimental diets were formulated to contain white fish meal (WFM) andvor BAIFA-M as the main animal protein source to determine the optimum BAIFA-M level to replace WFM protein. The diets contained 100% WFM + 0% BAIFA-M in the diet M$_0$ (control) . 70%, WFM+30%, BAIFA-M in the diet M$_{30}$, 55 % WFM+45 % BAIFA-M in the diet M$_{45}$, ; 40 % WFM+60 % BAIFA-M in the diet M$_{60}$. The four groups of rockfish (232 g), receiving the four different diets, were fed for 8 weeks. Groups receiving M$_0$, M$_{30}$ and M$_{45}$/ diets did not show significant (P>0.05) difference in growth and feed efficiency; however, the group fed on M$_{60}$/ showed significantly slower growth and lower feed efficiency than the others. Body composition showed no significant difference among the four dietary groups. WFM protein can be replaced by BAIFA-M up to 45 % in the diet of the rockfish.

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Inhibition of Lipopolysaccharide-stimulated Inflammatory Cytokine Production by LY303511 in Human Macrophagic THP-1 Cells

  • Kim, So-Hee;Paek, Yun-Woong;Kang, In-Chol
    • International Journal of Oral Biology
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    • v.42 no.3
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    • pp.117-121
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    • 2017
  • We have previously shown that the specific phosphatidylinositol 3-kinase inhibitor LY294002 (LY29), and its inactive analog LY303511 (LY30), inhibit a monocyte chemoattractant protein-1 (MCP-1) expression in human umbilical vein endothelial cells; these results suggest the potential of LY30 as an anti-inflammatory drug. In this study, we determined the effects of LY30 on the production of various inflammatory cytokines in human macrophagic THP-1 cells which were stimulated with lipopolysaccharide (LPS). LY30 selectively suppressed the mRNA expression of IL-12 p40, $TNF-{\alpha}$, and MCP-1 without affecting the expression of $IL-1{\alpha}$, IL-6, and IL-8. Inhibition of the production of IL-12 and $TNF-{\alpha}$ by LY30 was also demonstrated using ELISA assays. In order to elucidate the mechanisms of the action of LY30, we examined the role played by the mitogen-activated protein kinases and the key transcription factors, AP-1 and $NF-{\kappa}B$ in LPS-stimulated THP-1 cells. The results revealed that LY30 inhibited LPS-induced activation of ERK, but not p38 or JNK. Furthermore, the AP-1 DNA binding activity was suppressed by LY30 based upon the dosage, whereas $NF-{\kappa}B$ DNA binding was not affected. These results suggest that LY30 selectively inhibits cytokine production in the LPS-stimulated macrophagic THP-1 cells by down-regulating the activation of ERK and AP-1.

Changes in Taste Components of Marsh Calm Soup as Affected by Boiling Time (재첩국 제조시 가열시간에 따른 맛성분의 변화)

  • Chun, Soon-Sil;Suh, Jae-Soo;Oh, Chan
    • The Korean Journal of Food And Nutrition
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    • v.13 no.6
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    • pp.529-533
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    • 2000
  • The marsh calm soup was prepared with 2 volumes of boiling water and heated for 0, 5, 10, 30, 60 and 120 minutes. As the boiling time prolonged, water content decreased gradually, while protein content increased. Free amino acid content was the highest with 30 minutes of boiling showing 103.1 mg/100g, and decrease showly thereafter. Among the free amino acids, alanine was the most abundant followed by proline, glutamic acid and glycine. Degree of protein hydrolysis increased as boiling prolonged. In the non-volatile organic acids, succinic acid was the highest(137.08 mg/100g with 30 minutes of boiling), followed by oxalic acid, magic acid and lactic acid. The optimum boiling time for marsh calm soup was evaluated to be 30 minutes.

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Purification and Properties of Ribosome-inactivating Proteins from the Leaves of $Cucurbita\;moschata\;D_{UCHESNE}$ (호박$(Cucurbita\;moschata\;D_{UCHESNE})$잎에서 리보즘불활성화 단백질의 분리 및 특성)

  • Lee, Si-Myung;Kim, Yeong-Tae;Hwang, Young-Soo;Cho, Kang-Jin
    • Applied Biological Chemistry
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    • v.40 no.5
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    • pp.375-379
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    • 1997
  • Two ribosome-inactivating proteins, PRIP 1 and PRIP 2 have been isolated from the leaves of $Cucurbita\;moschata\;D_{UCHESNE}$. Crude extracts were purified through ammonium sulfate precipitation and column chromatography using DE-52 cellulose, S-Sepharose, FPLC Suprose 12 HR and FPLC Mono-S. The molecular weights of PRIP 1 and PRIP 2 were 31,000 and 30,500, respectively. PRIP 2 was thermostabe and maintained its activity even after the incubation of the protein at $50^{\circ}C$ for 30 min. In a cell free in vitro translation system using rabbit reticulocyte lysate, protein synthesis was inhibited by the addition of PRIP 1 and PRIP 2. The $IC_{50}$ of PRIP 1 and PRIP 2 were 0.82 nM and 0.79 nM, respectively. The comparison of N-terminal amino acid sequences of the PRIP 1 and PRIP 2 with known RIPs revealed that PRIP 1 shows sequence similarity with Luffin B from Luffa cylindrica and Trichokirin from Trichosanthes kirilowii Maximowicz and PRH) 2 has sequence similarity with Momordin II and MAP 30 from Momordica charantia.

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