• 제목/요약/키워드: 30K protein

검색결과 3,894건 처리시간 0.033초

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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    • 제30권6호
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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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중금속이 Cyanobacterium synechocystis sp.PCC 6803의 성장과 단백질 합성에 미치는 영향 (Effects of Heavy Metals on Growth and Protein Synthesis in Cyanobacterium synechocystis sp. PCC 6803)

  • 강경미;장남기
    • 아시안잔디학회지
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    • 제10권4호
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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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    • 제30권1호
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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.
    • 한국식물병리학회:학술대회논문집
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    • 한국식물병리학회 2003년도 정기총회 및 추계학술발표회
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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
    • 한국생물물리학회:학술대회논문집
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    • 한국생물물리학회 2002년도 제9회 학술 발표회 프로그램과 논문초록
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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
    • 한국양식학회지
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    • 제18권3호
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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
    • 한국양식학회지
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    • 제13권3호
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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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    • 제42권3호
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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.

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

  • 전순실;서재수;오찬
    • 한국식품영양학회지
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    • 제13권6호
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    • pp.529-533
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    • 2000
  • 본 실험에서는 재첩가공에 관한 기초자료를 제시할 목적으로, 제첩국 제조시 가열시간에 따른 맛 성분의 조성변화에 관해 실험하였다. 재첩국은 원료 중량 당 2배량의 끓는 물을 가하여 0, 5, 10, 30, 60및 120분간 가열하였다. 가열시간이 증가함에 따라 수분함량은 감소하였으며, 단백질함량은 점차로 증가하였다. 가열 시간 30분에서 유리아미노산의 함량은 103.10 mg/100 g으로 가장 높게 나타났으며, 30분 이후부터는 서서히 감소하였다. 유리아미노산 함량은 alanine의 함량이 가장 높았으며, 그 다음으로 proline, glutamic acid 및 glycine의 순이었다. 재첩국의 단백질 가수분해도는 가열시간 증가함에 따라 높게 나타났다. 비휘발성 유기산 함량은 succinic acid 함량이 가열시간 30분에서 137.08 mg/100 g으로 가장 높게 나타났으며, 그 다음은 oxalic aicd, magic aicd 및 lactic acid 순이었다. 따라서 재첩국 제조시 최적 가열시간은 30분이었다.

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

  • 이시명;김영태;황영수;조강진
    • Applied Biological Chemistry
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    • 제40권5호
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    • pp.375-379
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    • 1997
  • 리보즘불활성화 단백질(Ribosome-inactivating protein, RIP)을 생성하는 식물을 탐색하여 그중 호박$(Cucurbita\;moschata\;D_{UCHESNE})$ 잎에서 ammonium sulfate 침전, DE 52-Cellulose, S-Sepharose, FPLC Superose 12 HR, FPLC Mono-S column chromatography에 의하여 ribosome-Inactivating 활성이 있는 단백질(PR 1, PRIP 2)을 분리하였다. 정제된 단백질의 분자량은 SDS-PAGE에서 약 31,000과 30,500인 염기성 단백질로서, 특히 PRIP 1은 열에도 안정하여 $50^{\circ}C$에서 30분간 처리한 경우에도 활성이 유지되었다. 이 단백질들의 ribosome-inactivating 활성을 in vitro translation system에서 측정한 결과 50% 활성저해농도 $(IC_{50})$는 PRIP 1은 0.82nM, PRIP 2은 0.79 nM이었다. PRIP 1과 PRIP 2의 N-말단부분의 아미노산 서열을 분석하여, 이미 밝혀진 리보즘불활성화 단백질들과 아미노산서열의 유사성을 분석해 본 결과, PRIP 1은 Luffa cylindrica에서 분리된 Luffin B 및 Trichosanthes kirilowii Maximowicz에서 분리된 Trichokirin과, PRE 2은 Momordia charantia에서 분리된 Momordin II 및 MAP 30과 유사성이 매우 높았다.

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