• Title/Summary/Keyword: ${\gamma}/{\gamma}'$ structure

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${\gamma}$-FUZZY FILTER AND LIMIT STRUCTURE

  • Lee, Yoon-Jin
    • Proceedings of the Korean Institute of Intelligent Systems Conference
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    • 1998.06a
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    • pp.219-224
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    • 1998
  • We introduce the notion of ${\gamma}$-fuzzy filter and ${\gamma}$-limit structure to L-fuzzy point. We show that the category ${\gamma}$Lim of ${\gamma}$-limit spaces is a cartesian closed topological construct containing the category LFTop of stratified L-fuzzy topological spaces as a bireflective subcategory.

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Conformation and Biological Activity of the Neuropeptide $\gamma$ (Neuropeptide $\gamma$의 구조 및 생리활성)

  • Ku Hee-Jung;SEO Jung-Kil;KIM Eun-Hi;HUH Min-Do;CHUNG Joon-Ki;PARK Jang-Su;KANG Shin-Won;PARK Nam Gyu
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.30 no.2
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    • pp.244-251
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    • 1997
  • The relationship between structure and biological activity was studied on the three neuropeptides (mammalian, trout- and goldfish-neuropeptide $\gamma$) that were syntheized by the solid-phase method. Circular dichroism spectra showed that mammalian, trout- and goldfish-neuropeptide $\gamma$ adopted an unordered structure in buffer solution. In the-presence of neutral and acidic liposomes, mammalian and trout-neuropeptioe $\gamma$ also took a random structure. However, goldfish-neuropeptide $\gamma$ took an $\alpha-helical$ structure in acidic liposomes. The intestinal motility response was investigated with carp intestines, guinea-pig ileums and rat duodenums. In case of carp intestine, contractile activity was as follows : goldfish-neuropeptide $\gamma\simeq$ trout-neuropeptide $\gamma>$ mammalian-neuropeptide $\gamma$, On the other hand, the contractile activity of mammalian-neuropeptide $\gamma$ was more potent than trout- and goldfish-neuropeptide $\gamma$ in the guinea-pig ileums and rat duodenums. These results suggest that neuropeptide $\gamma$ show the species-specific activity.

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MOLECULAR CLONING OF CHICKEN INTERFERON-GAMMA (닭 인터페론 유전자의 클로닝에 관한 연구)

  • ;Hyun Lillehoj
    • Proceedings of the Korea Society of Poultry Science Conference
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    • 1999.11a
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    • pp.34-50
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    • 1999
  • A cDNA encoding chicken interferon-gamma (chIFN-${\gamma}$) was amplified from P34, a CD4$^{+}$ T-cell hybridoma by reverse transcription-polymerase chain reaction (RT-PCR) and cloned into pUC18. THe sequences of cloned PCR products were determined to confirm the correct cloning. Using this cDNA as probe, chicken genomic library from White Leghorn spleen was screened. Phage clones harboring chicken interferon-gamma (chIFN-${\gamma}$) were isolated and their genomic structure elucidated. The chIFN-${\gamma}$ contains 4 exons and 3 introns spanning over 14 kb, and follows the GT/AG rule for correct splicing at the exon/intron boundaries. The four exons encode 41, 26, 57 and 40 amino acids, respectively, suggesting that the overall structure of IFN-${\gamma}$ is evolutionairly conserved in mammalian and avian species. The 5’-untranslated region and signal sequences are located in exon 1. Several AT-rich sequences located in the fourth exon may indicate a role in mRNA turnover. The 5’-flanking region contains sequences homologous to the potential binding sites for the mammalian transcription factors, activator protein-1(AP-1) activator protein-2(AP-2) cAMP-response element binding protein(CREB), activating transcription factor(ATF), GATA-binding fator(GATA), upstream stimulating factor(USF), This suggests that the mechanisms underlying transcriptional regulation of chicken and mammalian IFN-${\gamma}$ genes may be similar.r.

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Structure and Contractile Activity of the Bowfin- and Shark-neuropeptide $\gamma$ (Bowfin-과 Shark-neuropeptide $\gamma$의 구조 및 수축효과)

  • KIM Eun Jung;SEO Jung-Kil;KIM Chan-Hee;GO Hye-Jin;HUH Min-Do;MOON Jung-Hye;PARK Jang-Su;PARK Nam Gyu
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.32 no.2
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    • pp.232-237
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    • 1999
  • The relationship between structure and contractile activity was studied on the three neuropeptide $\gamma$ (mammalian-, bowfin-, shark-NP$\gamma$) that were synthesized by the solid-phase method. Circular dichroism spectra showed that mammalian-, bowfin- and shark-neuropeptide $\gamma$ took an unordered structure in buffer solution and artificial liposome. The intestinal motility response was investigated with guinea-pig ileum, rat duodenum and carp intestine. In case of carp intestine, contractile activity was as follows; bowfin-NP$\gamma$> shark-NP$\gamma$>mammalian-NP$\gamma$, On the other hand, the contractile activity of mammalian-neuropeptide $\gamma$ was more potent than those of bowfin-, shark-neuropeptide $\gamma$ in the guinea-pig ileum and rat duodenum. These results suggest that NP$\gamma$ show the species-specific activity.

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Investigation of γ/γ' Growth by Macro Segregation in the Ni-Base Single Crystal Superalloy, CMSX-10 (CMSX-10 단결정 초내열합금에서 거시편석에 따른 γ/γ' 응고조직 형성)

  • Yoon, Hyeyoung;Sung, Changhoon;Shin, Jongho;Han, Seong Zeon;Lee, Jehyun
    • Korean Journal of Materials Research
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    • v.25 no.9
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    • pp.435-441
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    • 2015
  • The ${\gamma}/{\gamma}^{\prime}$ two-phases, commonly known as a eutectic structure, are observed in the ${\gamma}$ interdendritic region of a Ni-base superalloy. However, the growth behavior of the ${\gamma}/{\gamma}^{\prime}$ two-phases, whether it is of eutectic or peritectic nature, has not been decidedly established. Directional solidifications were, thus, performed with the planar interface at a low growth rate of $0.5{\mu}m/s$ in order to promote macro segregation. Directional solidification started with the ${\gamma}$ planar interface and the ${\gamma}^{\prime}$ phase nucleated on the ${\gamma}$ planar interface at the solidification fraction of 0.75. The ${\gamma}/{\gamma}^{\prime}$ two-phases showed the ${\gamma}^{\prime}$ rod structure as major phase and the ${\gamma}$ minor phase between ${\gamma}^{\prime}$ rods, and the volume fraction of the ${\gamma}$ phase changed continuously with an increasing solidification fraction. The two-phase ${\gamma}/{\gamma}^{\prime}$ is seen as the coupled peritectic.

글루타치온 생산효소( $\gamma$-Glutamylcysteine Synthetase)와 그 변이효소의 구조분석 및 반응 Kinetics 연구

  • Yang, Hye-Jeong;Gwon, Dae-Yeong
    • Bulletin of Food Technology
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    • v.17 no.4
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    • pp.98-106
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    • 2004
  • Two mutant enzymes of $\gamma$-glutamylcysteine synthetase ($\gamma$-GCS) which catalyzed the synthesis of $\gamma$-glutamylcysteine from L-glutamic acid and L-cysteine in the presence of ATP, were prepared bypoint mutation of $\gamma$-GCS gene with site-directed mutagensis in E. coli. Conformational structuresand catalytic reaction kinetics of mutant enzymes were compared with wild type $\gamma$-GCS afterpurification. The S495F mutant enzyme (serine at 495 residue was substituted with phenylalanine),which had no catalytic activity for $\gamma$-glutamylcysteine synthesis, rarely folded even in neutral pH.However, the mutant A494V (alanine of 494 residue was replaced by valnine) which showed 50 %increase of activity, had a high folding structure. The folding structure of A494V also more stable athigh temperature and extreme pH compared to wild type and S495F. Reaction kinetics of wild typeand A494V were also investigated, Km value of A494V was smaller than that of wild type, while itshowed a little difference at Vmax values. This result evolved that alanine at 494 may be involved inbinding site of substrate rather than catalytic site. In addition, change of catalytic activity by onepoint mutation was highly correlated with the folding structure of enzyme.

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STRUCTURES OF INVOLUTION Γ-SEMIHYPERGROUPS

  • Yaqoob, Naveed;Tang, Jian;Chinram, Ronnason
    • Honam Mathematical Journal
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    • v.40 no.1
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    • pp.109-124
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    • 2018
  • In this paper, structure of involution ${\Gamma}$-semihypergroup is introduced and some theorems about this concept are stated and proved. The concept of ${\Gamma}$-hyperideal in involution ${\Gamma}$-semihypergroup is defined and some of their properties are studied. Some results on regular ${\Gamma}^*$-semihypergroups and fuzzy ${\Gamma}^*$-semihypergroups are also provided.

Solution Structure of Neuropeptide $\gamma$ from Carassius auratus by NMR spectroscopy

  • Lee, Sangwon;Park, Namgyu;Kim, Yangmee
    • Proceedings of the Korean Biophysical Society Conference
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    • 1999.06a
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    • pp.31-31
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    • 1999
  • Neuropeptide ${\gamma}$ is a recently identified tachykinin family peptide which has conserved ammo acid sequence of -Phe-X-Gly-Leu-Met-NH2 in the C-terminal region, where X represents aromatic or hydrophobic residues. In this study, three-dimensional structure of neuropeptide ${\gamma}$ from goldfish Carassius auratus (G-NP${\gamma}$) was determined by NMR spectroscopy.(omitted)

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Effect of Gamma-Irradiation on the Molecular Properties of Blood Plasma Proteins

  • Song, Kyung-Bin;Lee, Seunghwan;Lee, Seunghyun
    • Preventive Nutrition and Food Science
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    • v.7 no.2
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    • pp.184-187
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    • 2002
  • Blood products from slaughterhouses that are not hygienically prepared for disposal or food consumption pose a human health hazard. Gamma irradiation is an effective method for sterilization of blood products, but may introduce changes in the molecular characteristics of proteins. This study evaluated the effects of irradiation on animal plasma proteins. Bovine and porcine blood was obtained from a slaughterhouse and the plasma proteins purified and lyophilized. The secondary structure and molecular weight distribution of the plasma protein solutions and powders were examined after ${\gamma}$-irradiation at 1, 5, 7 and 10 kGy. Gamma-irradiation affected the molecular properties of the protein solutions, but not the protein powders. Circular dichroism and sodium dodecyl sulfate-polyacrylamide gel electrophoresis studies showed that increased doses of ${\gamma}$-irradiation decrease the ordered structure of plasma proteins in solution, and cause initial fragmentation of the polypeptide chains and subsequent aggregation.

The crystal and molecular structure of $\gamma$-hydroxy-.$\beta$-amino butyric acid

  • Kim, Yang-Bae
    • Archives of Pharmacal Research
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    • v.8 no.1
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    • pp.1-6
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    • 1985
  • The crystal structure or $\gamma$-hydroxy-$\betha$-aminobutyric acid was determined by MULTAN system with X-ray intensity data on a diffractometer and refined by the least-squares method to an R-value 0.034 for 711 reflections. The crystals were orthorhombic, space group $P2_{1}2_{1}2_{1}$, Z = 4, with a = 10.220, b = 8.257 and c = 6.556$\AA$. The molecule takes the zwitterionic form and skeletal conformation is trans-transform. The molecules are held together by intra-and intermolecular NH-O and OH--O hydrogen bonds.

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