• 제목/요약/키워드: specific protein

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클로람페니콜 내성 플라스미드 pKH7의 Pre 단백질의 염기서열 결정 (Nucleotide Sequence of Pre Protein in Chloramphenicol Resistance Plasmid pKH7.)

  • 문경호;박봉동;이동석;이백락
    • 한국미생물·생명공학회지
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    • 제26권6호
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    • pp.566-568
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    • 1998
  • Partial nucleotide sequence (nt 1-1842) of chloramphenicol resistance plasmid pKH7 has been reported previously and residual nucleotide sequence (nt 1843-4118) of pKH7 was determined and then the complete nucleotide sequence of pKH7 was obtained. pKH7 consists of 4118 bp and has three ORFs. Besides Rep and CAT proteins described in previous paper, Pre protein which mediates site-specific recombination in Staphylococcus aureus was found to be on pKH7. R $S_{A}$, a site-specific recombination site of Pre protein, and palA, a specific lagging-strand conversion signal, was also found in pKH7. Amino acid sequence of Pre protein of pKH7 was compared with those of other antibiotic resistant Staphylococcus aureus plasmids.s.

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The 10 kDa protein of Taenia solium metacestodes shows genus specific antigenicity

  • Park, Seung-Kyu;Yun, Doo-Hee;Chung, Joon-Yong;Kong, Yoon;Cho, Seung-Yull
    • Parasites, Hosts and Diseases
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    • 제38권3호
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    • pp.191-194
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    • 2000
  • Genus specific antigenicity of the 10 kDa protein in cyst fluid (CF) of Taenia solium metacestodes was demonstrated by comparative immunoblot analysis. When CFs from taeniid metacestodes of T. saginata, T. solium, T. taeniaeformis and T. crassiceps were probed with specific monoclonal antibody (mAb) raised against 150 kDa protein of T. solium metacestodes, specific antibody reactions were observed in 7 and 10 kDa proteins of T. solium and in 7/8 kDa of T. saginata, T. taeniaeformis and T. crasiceps. The mAb did not react with any protein in hydatid fluid of Echinococcus granulosus and E. multilocularis. This result revealed that the 10 kDa peptide of T. solium metacestodes and its equivalent proteins of different Taenia metacestodes are genus specific antigens that are shared among different Taenia species.

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Identifying Responsive Functional Modules from Protein-Protein Interaction Network

  • Wu, Zikai;Zhao, Xingming;Chen, Luonan
    • Molecules and Cells
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    • 제27권3호
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    • pp.271-277
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    • 2009
  • Proteins interact with each other within a cell, and those interactions give rise to the biological function and dynamical behavior of cellular systems. Generally, the protein interactions are temporal, spatial, or condition dependent in a specific cell, where only a small part of interactions usually take place under certain conditions. Recently, although a large amount of protein interaction data have been collected by high-throughput technologies, the interactions are recorded or summarized under various or different conditions and therefore cannot be directly used to identify signaling pathways or active networks, which are believed to work in specific cells under specific conditions. However, protein interactions activated under specific conditions may give hints to the biological process underlying corresponding phenotypes. In particular, responsive functional modules consist of protein interactions activated under specific conditions can provide insight into the mechanism underlying biological systems, e.g. protein interaction subnetworks found for certain diseases rather than normal conditions may help to discover potential biomarkers. From computational viewpoint, identifying responsive functional modules can be formulated as an optimization problem. Therefore, efficient computational methods for extracting responsive functional modules are strongly demanded due to the NP-hard nature of such a combinatorial problem. In this review, we first report recent advances in development of computational methods for extracting responsive functional modules or active pathways from protein interaction network and microarray data. Then from computational aspect, we discuss remaining obstacles and perspectives for this attractive and challenging topic in the area of systems biology.

인시목 곤충의 성충체액단자질에 관한 생리성화학적 연구 1. 가잠의 성충특이체액단자질의 검출 (Physiological and Biochemical Studies on the Adult Hemolymph proteins in Lepidoptera. 1. Appearance of Adult Specific Proteins in the Hemolymph of the Silkworm, Bombyx mori.)

  • 성주일;문재유
    • 한국잠사곤충학회지
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    • 제30권1호
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    • pp.20-24
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    • 1988
  • 누에의 우화와 함께 새로이 출현하는 성충특이체액단자질(ASP-I, ASP-II)의 검출, 성특이성, 품종간 분포 및 변이성에 관하여 PAGE 전기영동법을 이용 실험한 결과, 1. 우화와 함께 알, 유충, 번데기의 발육시기에는 출현하지 않는 2가지의 새로운 성충특이단자질 영동대가 검출되었으며, 이동도가 느린 영동대를 ASP-I(Adult specific protein of slow mobility), 빠른 영동대를 ASP-II(Adult specific protein of slow mobility)로 명명하였다. 2. 성충특이체액단자질(ASP-I, ASPII)은 성특이성이 없었다. 3. 실험에 사용된 모든 누에 품종의 성충체액에서 ASP-I 및 ASP-II가 검출되었으나, 품종간의 변이성은 인정되지 않았다.

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돼지 췌장내 Protein Methylase I의 분리정제 및 성질 (Purification and Properties of Protein Methylase I from Hog Pancreas)

  • 이향우;장만식
    • 약학회지
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    • 제31권3호
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    • pp.173-181
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    • 1987
  • Protein methylase I has been partially purified from hog pancreas with a 11% yeild. The final preparation is completely free of any other protein-specific methyltransferases and endogenous substrate proteins. The enzyme has an optimum pH of 7.2 and the approximate molecular weight is above 800 thousands dalton. The Km values for S-adenosyl-L-methionine and histone type II-A are 1.32$\times$10$^{-5}$M. The Ki value for S-adenosyl-L-homocysteine is 1.52$\times$10$^{-6}$M. The effect of enyzme concentration on the activity showed a slight sigmoidal curve suggesting the involvement of certain cofactors. Even though the purified enzyme showed two bands on polyacrylamide gel electrophoresis, the enzyme is highly specific for the arginine residues of protein and specifically, highly specific for histone, suggesting histonespecific protein methylase I.

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육가공품(肉加工品)중 단백질의 전기영동(電氣泳動) 패턴 (Electrophoretic Pattern of Specific Proteins in Meat Products)

  • 이정희;이서래
    • 한국식품과학회지
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    • 제20권1호
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    • pp.34-39
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    • 1988
  • 여러가지 육가공품(肉加工品)중 특정 단백질 원료의 첨가여부를 판정하여 변조식품(變造食品)을 검출하는 한 방법으로서, 각종 육류단백질, non-meat protein, 어육(魚肉)가공품을 대상으로 disc SDS-Poly acrylamide gel electrophoresis의 사용 가능성을 실험하였다. Total protein fraction에 대한 전기영동 결과 복잡하고 많은 band를 보여 각 시료에 고유한 특성을 찾아보기 어려웠다. Low salt-soluble protein fraction에서는 total protein fraction 에서 보다 band 수가 상당히 감소함을 보였고 각 단백질 원료에 대하여 보다 고유한 band pattern을 나타내었다. Acetone-insoluble protein fraction 에서는 non-meat protein의 경우 육류단백질과 상당히 다른 경향을 나타내었고. 소세지 원료의 가열처리에 의하여 단백질의 band수와 양이 감소하였다. 따라서 적당한 단백질 추출조건(抽出條件)을 설정하여 전기영동을 실시하면, 특정(特定) 단백질을 첨가한 변조식품의 검출이 가능해질 것으로 생각된다.

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Site-Specific Labeling of Proteins Using Unnatural Amino Acids

  • Lee, Kyung Jin;Kang, Deokhee;Park, Hee-Sung
    • Molecules and Cells
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    • 제42권5호
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    • pp.386-396
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    • 2019
  • Labeling of a protein with a specific dye or tag at defined positions is a critical step in tracing the subtle behavior of the protein and assessing its cellular function. Over the last decade, many strategies have been developed to achieve selective labeling of proteins in living cells. In particular, the site-specific unnatural amino acid (UAA) incorporation technique has gained increasing attention since it enables attachment of various organic probes to a specific position of a protein in a more precise way. In this review, we describe how the UAA incorporation technique has expanded our ability to achieve site-specific labeling and visualization of target proteins for functional analyses in live cells.

지렁이(Lumbricus terrestris)로부터 Thiol-Specific Antioxidant protein(TSA)의 분리 및 정제에 관한 연구 (Purification and Characterization of TSA from Lumbricus terrestris)

  • 곽병구;김일한;차미경
    • 자연과학논문집
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    • 제14권2호
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    • pp.55-65
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    • 2004
  • 지렁이(Earthworm, Lumbricus terrestris)로부터 thiol-specific antioxidant activity(TSA)를 나타내는 향산화 단백을 분리정제 하였다. 이 향산화 단백은 환원제로 thiol성분에 의해 유지되는 비효소적 금속 촉매 산화계 (MCO, $Fe^{3+}$, DTT 또는 2-mercatoethanol ; Thiol- MCO system)에 의하여 Glutamine Synthetase의 불활성을 억제하지만 아스코르브산과 같은 nonthiol 환원제를 가진 효소적 금속 촉매 산화계 (MCO, $Fe^{3+}$, ascorbate ; nonthiol- MCO system)에서는 Glutamine Synthetase의 불활성을 방어하지 못하였다. 정제된 지렁이 TSA 단백질은 SAS-PAGE에 의해 51-kDa임을 밝혔고, 기존에 알려진 TSA protein과 분자량이 다른 TSA Family로써 활성 산소종에 의한 산화적 손상을 방어하는 향산화 효소로써의 중요한 생화학적 역할을 수행함을 제시하였다.

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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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    • 제34권6호
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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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Effects of Specific Interaction Altering Reagents on Hardnesses of Succinylated Soy Protein Gel

  • Bae, Dongho;Jung, Hosun;Choi, Yong-Hee
    • Journal of Applied Biological Chemistry
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    • 제42권3호
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    • pp.125-129
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    • 1999
  • The changes in gel characteristics of soy protein and succinylated soy protein due to various specific interaction-altering reagents which affect the formation and textural properties of gels, were studied. The reagents were added to 15% soy protein solutions prior to heat treatment. Succinylated soy protein formed harder gel without the addition of reagents. Hardly no gels were formed with urea, indicating that hydrogen bonds significantly contributed to the formation and hardness of the gel and the effects of urea on the hardness of succinylated soy protein gel were more significant. Disulfide bonds were important in the formation of hard gels whether they were succinylated or not, but the contributions of hydrophobic interactions to gel hardness were relatively insignificant. The hardness reducing effects of NaCl and NaSCN were more significant in succinylated soy protein gel. As such, electrostatic interactions were important for succinylated soy protein to form hard gel but not for unmodified soy protein.

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