• Title/Summary/Keyword: 28S

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Genetic Characterization based on Partial 28S rRNA Gene Sequence of Korean Two Scallops (한국산 가리비 2종의 28S rRNA 유전자 염기서열에 의한 유전적 특성)

  • Park, Gab-Man
    • The Korean Journal of Malacology
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    • v.13 no.1
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    • pp.1-7
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    • 1997
  • 한국산 가리비, 큰가리비(Patinopecten yessoensis)와 주문진가리비(Chlamys swifti), 2종에 대한 28S ribosomal RNA 유전자의 PCR- 산물을 이용 RFLP 및 염기서열을 밝히고, 이미 보고된 2과 3종의 염기서열과 상동성을 비교 분석하였다. 그 결과 28S rRNA유전자를 이용하여 7가지 제한효소를 처리한 PCR-RFLP의 종간 차이에서 Taq I 제한효소에서만 차이를 볼 수 있었다. 한편 두종간에 28S rRNA유전자의 D1 부위의 염기서열에서 231개 부위 중 14군데에서 변이를 보였다.

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Responsivity of IRTS/FILM in Orbit

  • Oh S.H.;Nakagawa T.;Kwon S.M.;Pak S.;Lee H.M.;Jeong W.S.;Makiuti S.;Pearson C.
    • The Bulletin of The Korean Astronomical Society
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    • v.28 no.2
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    • pp.28-28
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    • 2003
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Analysis of antigenic domain of GST fused major surface protein (p30) fragments of Toxoplasma gondii (융합단백질로 발현된 톡소포자충의 주요막단백질(p30) 절편의 항원성)

  • 남호우;임경심
    • Parasites, Hosts and Diseases
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    • v.34 no.2
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    • pp.135-142
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    • 1996
  • Antigenic domain of jai or surface protein (p30) of Toxoplosmc Sondii was analyzed after polymerase chain reaction (PCR) of its gene fragments. Hydrophilic or hydrophobic moiety of amino acid sequences were expressed as glutathione S-transferase (G57) fusion proteins. Fragments of p30 gene were as follows: 737, total p30 open reading frame (ORF) ; S28, total ORF excluding N-terminal signal sequence and C-terminal hydrophobic sequence; Al9, N-terminal 2/3 parts of A28; A19, N-terminal 2/3 of S28; P9, C-terminal 2/3 part of S28; Z9. middle 1/3 of S28; and 29, C-terminal 1/3 of S28. respectively. Primer of each fragment was synthesized to include clamp sequence of EcoR I restriction site. PCR amplified DNA was inserted info GST (26 kDa) expression vector, PGEX-47-1 to transform into Escheri,hia coei (.JM105 strain). G57 fusion proteins were expressed with IPTG induction as 63. 54, 45, 45, 35, 36. and 35 kDa proteins measured by SDS-PAGE. Each fusion protein was confirmed with G57 detection kit. Western blot analysis with the serum of a toxoplasmosis patient revealed antigenicity in proteins expressed by T37. S28, and Al9 but not those by Pl8. X9, Y10, and Z9. Antigenicity of p30 seems to be located either in N-terminal 115 part in the presence of middle 1/3 part or in the oligopeptides between margins of the first and second 1/3 parts.

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Molecular Systematics of the Tephritoidea (Insecta: Diptera): Phylogenetic Signal in 16S and 28S rDNAs for Inferring Relationships Among Families

  • Han, Ho-Yeon;Ro, Kyung-Eui;Choi, Deuk-Soo;Kim, Sam-Kyu
    • Animal cells and systems
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    • v.6 no.2
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    • pp.145-151
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    • 2002
  • Phylogenetic signal present in the mitochondrial 16S ribosomal RNA gene (16S rDNA) and the nuclear large subunit ribosomal RNA gene (28S rDNA) was explored to assess their utility in resolving family level relationships of the superfamily Tephritoidea. These two genes were chosen because they appear to evolve at different rates, and might contribute to resolve both shallow and deeper phylogenetic branches within a highly diversified group. For the 16S rDNA data set, the number of aligned sites was 1,258 bp, but 1,204 bp were used for analysis after excluding sites of ambiguous alignment. Among these 1,204 sites, 662 sites were variable and 450 sites were informative for parsimony analysis. For the 28S rDNA data set, the number of aligned sites was 1,102 bp, but 1,000 bp were used for analysis after excluding sites of ambiguous alignment. Among these 1000 sites, 235 sites were variable and 95 sites were informative for parsimony analysis. Our analyses suggest that: (1) while 16S rDNA is useful for resolving more recent phylogenetic divergences, 28S rDNA can be used to define much deeper phylogenetic branches; (2) the combined analysis of the 16S and 28S rDNAs enhances the overall resolution without losing phylogenetic signal from either single gene analysis; and (3) additional genes that evolve at intermediate rates between the 16S and 28S rDNAs are needed to further resolve relationships among the tephritoid families.

Coming To America: The Use of 28 U.S.C. § 1782

  • Robertson, Ann Ryan;Friedman, Scott L.
    • Journal of Arbitration Studies
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    • v.25 no.3
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    • pp.59-90
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    • 2015
  • Since 1855, the federal courts of the United States have been empowered to assist in the gathering of evidence for use before foreign tribunals. Today, the source of that authority is 28 U.S.C. ${\S}1782$ which permits the courts to order a person "to give [ ] testimony... or to produce a document ... for use in a proceeding in a foreign or international tribunal${\cdots}$ ." It was generally assumed, until the United States Supreme Court's decision of Intel Corp. v. Advanced Micro Devices, Inc. in 2004, that arbitration tribunals were not "foreign tribunals" for purposes of 28 U.S.C. ${\S}1782$. While the issue in Intel did not involve an arbitration tribunal, a statement by the Supreme Court in dicta has called into question the exact parameters of the words "foreign tribunal," resulting in a split of opinion among the federal courts of the United States. This article explores the legislative history of 28 U.S.C. ${\S}1782$, examines the United States Supreme Court decision in Intel, and discusses the split among the courts of the United States regarding the interpretation of "foreign tribunal." The article further surveys emerging issues: is an arbitration tribunal in a case involving foreign parties and seated in the United States a "foreign tribunal"; does agreeing to the use of the IBA Rules on the Taking of Evidence in International Arbitration circumscribe the use of 28 U.S.C. ${\S}1782$; can a party be ordered to produce documents located outside the United States; and is there a role for judicial estoppel in determining whether an application pursuant to 28 U.S.C. ${\S}1782$ should be granted?

Comparison of Nucleotide Sequences of 28S rDNA from Two Viviparid Snail Species in Korea : Cipangopaludina chinensis malleata and C. Japanica (한국산 논우렁이와 큰논우렁이의 28S rDNA 유전자 염기서열 분석)

  • Park, Gab-Man;Younghun Jung;Kim, Jae-Jin;Chung, Pyung-Rim
    • The Korean Journal of Malacology
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    • v.13 no.2
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    • pp.91-96
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    • 1997
  • 한국산 논우렁이(CIpangopaludina chinensis malleata)와 큰논우렁이 (C. japomica)는 형태학적으로 유사하여 그 감별이 용이치 않다. 본 연구는 이 두 종을 대상으로 28S rDNA DI유전자를 7종의 제한효소로 처리하여 PCR-RDLP기법으로 그 절편을 비교하였다. 절편 상호간에는 차이점을 관찰할 수 없었으나, 두 종으로부터 분석된 28S rDNA DI 유전자의 염기서열에서는 4 부위에서 종간 차이를 보였다.

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Nuclear rDNA characteristics for DNA taxonomy of the centric diatom Chaetoceros (Bacillariophyceae)

  • Oh, Hye-Young;Cheon, Ju-Yong;Lee, Jin-Hwan;Hur, Sung-Bum;Ki, Jang-Seu
    • ALGAE
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    • v.25 no.2
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    • pp.65-70
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    • 2010
  • The genus Chaetoceros provides highly diversified diatoms in marine systems. Morphological descriptions of the genus are well-documented, yet the DNA taxonomy of Chaetoceros has not been satisfactorily established. Here, the molecular divergences of the 18S-28S rDNA of Chaetoceros were assessed. DNA similarities were relatively low in both 18S (93.1 $\pm$ 3.9%) and 28S rDNA (81.0 $\pm$ 4.6%). Phylogenies of the 18S, 28S rDNAs showed that Chaetoceros was divided according to individual species, clustering the same species into single clades. Statistical analysis with corrected genetic (p-) distance scores showed that nucleotide divergence of Chaetoceros 28S rDNA significantly differed from that of 18S rDNA (Student's t-test, p < 0.05). This finding suggests that the 28S rDNA may be treated as a more suitable marker for species-level taxonomic distinctions of Chaetoceros.

Molecular phylogeny of parasitic Platyhelminthes based on sequences of partial 28S rDNA D1 and mitochondrial cytochrome c oxidase subunit I

  • Lee, Soo-Ung;Chun, Ha-Chung;Huh, Sun
    • Parasites, Hosts and Diseases
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    • v.45 no.3
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    • pp.181-190
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    • 2007
  • The phylogenie relationships existing among 14 parasitic Platyhelminthes in the Republic of Korea were investigated via the use of the partial 28S ribosomal DNA (rDNA) D1 region and the partial mitochondrial cytochrome c oxidase subunit 1 (mCOI) DNA sequences. The nucleotide sequences were analyzed by length, G + C %, nucleotide differences and gaps in order to determine the analyzed phylogenie relationships. The phylogenie patterns of the 28S rDNA D1 and mCOI regions were closely related within the same class and order as analyzed by the PAUP 4.0 program, with the exception of a few species. These findings indicate that the 28S rDNA gene sequence is more highly conserved than are the mCOI gene sequences. The 28S rDNA gene may prove useful in studies of the systematics and population genetic structures of parasitic Platyhelminthes.

Ability for Biosynthesis of C27 Brassinosteroids by an Enzyme Pool Prepared from Cultured Cells of Phaseolus vulgaris (강낭콩 현탁배양세포에서 추출된 Enzyme Pool의 C27 Brassinosteroids 합성 능력)

  • Kim Tae-Wuk;Joo Se-Hwan;Kim Seong-Ki
    • Journal of Plant Biotechnology
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    • v.32 no.1
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    • pp.63-71
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    • 2005
  • A cell-free enzyme solution prepared from suspension cultured cells of Phaseolus vulgaris successfully mediated conversions of cholesterol $\to$ cholestanol and 6-deoxo-28-norteasterone $\leftrightarrow$ 6-deoxo-28-nor-3-dehydroteasterone $\leftrightarrow$ 6-deoxo-28-nortyphasterol $\to$ 6-deoxo-28-norcastasterone $\to$ 28-norcastasterone. Al-though conversion of cholestanol to 6-deoxo-28-norteasterone intermediated by 6-deoxo-28-norcathasterone was not demonstrated, this strongly suggests that a complete set of biosynthetic enzymes catalyzing reactions from cholesterol to 28-norcastasterone via 6-deoxo-28-nor type brassinosteroids is endogenously present in the cells, which demonstrates that a $C_{27}$ brassinosteroids biosynthetic pathway, namely the late C-6 oxidation for $C_{27}$ brassinosteroids, is operative in the cells. Additionally, the enzyme solution mediated conversion of 28-norcastasterone to castasterone in the presence of S-adenosyl-methionine and NADPH, providing that the $C_{27}$ brassinosteroids biosynthesis is an important route to generate castasterone in the cells. Together with our previous finding that castasterone can be biosynthesized by the same biosynthetic pathway in tomato, this study demonstrates that the $C_{27}$ brassinosteroids biosynthesis is a common alternative process to maintain endo-genous level of castasterone, an active $C_{28}$ brassinosteroid, in plants.