• Title/Summary/Keyword: Homogeneity-range

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Structural Characterization of the Intermetallic Phase EuZnxIn4-x (x ≈ 1.1-1.2). Zn and In Site-Preferences in the BaAl4 Structure-Type from Computational Analysis

  • You, Tae-Soo;Nam, Gnu;Kim, Youngjo;Darone, Gregory M.;Bobev, Svilen
    • Bulletin of the Korean Chemical Society
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    • v.34 no.6
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    • pp.1656-1662
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    • 2013
  • The ternary phase $EuZn_xIn_{4-x}$ has been identified as the main product of reactions of Eu, Zn, and In by using the In-flux method and characterized by both powder and single-crystal X-ray diffraction. The structure belongs to the common $BaAl_4$-type (tetragonal space group I4/mmm, Pearson code tI10) with lattice parameters of a = 4.5610(9) ${\AA}$, c = 12.049(3) ${\AA}$ for composition $EuZn_{1.10(12)}In_{2.90}$ and a = 4.5463(3) ${\AA}$, c = 12.028(2) ${\AA}$ for composition $EuZn_{1.18(2)}In_{2.82}$, respectively. In this structure, the Eu atoms are situated at the center of 18-vertex Fedorov polyhedra made of Zn and In atoms, where the 4d site is preferentially occupied by In and the 4e site is occupied by randomly mixed Zn and In atoms. Theoretical investigations using tight-binding linear muffintin orbital (TB-LMTO) method provide rationale for the observed site preferences and suggest potentially wider homogeneity range than the experimentally established for $EuZn_xIn_{4-x}$ ($x{\approx}1.1$).

Application of multimodal surfaces using amorphous silicon (a-Si) thin film for secondary ion mass spectrometry (SIMS) and laser desorption/ionization mass spectrometry (LDI-MS)

  • Kim, Shin Hye;Lee, Tae Geol;Yoon, Sohee
    • Proceedings of the Korean Vacuum Society Conference
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    • 2016.02a
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    • pp.384.1-384.1
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    • 2016
  • We reported that amorphous silicon (a-Si) thin film provide sample plate exhibiting a multimodality to measure biomolecules by secondary ion mass spectrometry (SIMS) and laser desorption/ionization mass spectrometry (LDI-MS). Kim et al.1 reported that a-Si thin film were suitable to detect small molecules such as drugs and peptides by SIMS and LDI-MS. Recently, bacterial identification has been required in many fields such as food analysis, veterinary science, ecology, agriculture, and so on.2 Mass spectrometry is emerging for identifying and profiling microbiology samples from its advantageous characters of label-free and shot-time analysis. Five species of bacteria - S. aureus, G. glutamicum, B. kurstaki, B. sphaericus, and B. licheniformis - were sampled for MS analysis without lipid extraction in sample preparation steps. The samples were loaded onto the a-Si thin film with a thickness of 100 nm which did not only considered laser-beam penetration but also surface homogeneity. Mass spectra were recorded in both positive and negative ionization modes for more analytical information. High reproducibility and sensitivity of mass spectra were demonstrated in a mass range up to mass-to-charge ratio(m/z) 1200 by applying the a-Si thin film in mentioned above MS. Principle component analysis (PCA) - a popular statistical analysis widely used in data processing was employed to differentiate between five bacterial species. The PCA results verified that each bacterial species were readily distinguished and differentiated effectively from our MS approach. It shows a new opportunity to rapid bacterial profiling and identification in clinical microbiology. More details will be discussed in the presentation.

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A Meta-Analysis of Explanatory Variables of Health Promotion Behavior (건강증진행위 설명요인에 대한 메타분석)

  • Park, Young-Joo;Lee, Sook-Ja;Park, Eun-Sook;Ryu, Ho-Shin;Lee, Jae-Won;Chang, Sung-Ok
    • Journal of Korean Academy of Nursing
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    • v.30 no.4
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    • pp.836-846
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    • 2000
  • This Meta-Analysis of 18 studies was conducted to determine the magnitude of th relationship between health promotion behavior and each of explanatory variables. The studies were measured using Health Promoting Life Style(HPLP) developed by Walker and others based on Pender's definiton of health promoting behavior. The sample was collected by searching for The Journal of Korean Academy Nursing Society, The Journal of Korean Women's Health Nursing Academic Society,The Journal of Korean Academic Society of Adult Nursing, Journal of Korean Community Nursing, The Journal of Fundamentals of Nursing, The Journal of Korean Nursing Administration Academic Society, The Korean Journal of Child Health Nursing, The Journal of Korean Psychiatric Academic Society, the dissertations for mater degree or doctoral dissertations for the period from 1980 to 1998. The explanatory variables measured more than 2 times in studies were self-efficacy, perceived health status, self-esteem, internal, powerful-others and chance dimensions of health locus of control, perceived benefits, hardiness, wellbeing and clinical demensions of health concepts, and quality of life(life satisfaction). Effect sizes were calculated by unweighted mean r, weighted mean r by sample size and weighted mean r by quality index score after homogeneity test. The mean r effect size indicator range of each predictor variable were as follows; quality of life (0.50- 0.52), self-efficacy (0.46-0.47), hardiness (0.42-0.44), self-esteem(0.41-0.43), health locus of control- internal(0.32-0.34), health locus of control- powerful others (0.25-0.31), perceived health status(0.18-0.19) and clinical dimensions of health concepts (0.16-0.17).

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Characterization of an Alkaline Protease from an Alkalophilic Bacillus pseudofirmus HS-54 (호알칼리성 Bacillus pseudofirmus HS-54가 생산하는 알칼리성 Protease의 특성)

  • Bang, Seong-Ho;Jeong, In-Sil
    • Korean Journal of Microbiology
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    • v.47 no.3
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    • pp.194-199
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    • 2011
  • An alkalophilic bacterium producing alkaline protease was isolated from waste water and solar saltern sample and identified as Bacillus pseudofirmus HS-54 based on morphological, biochemical characteristics as well as 16S-rRNA gene sequencing. The HS-54 protease was purified to homogeneity using ammonium sulfate precipitation, DEAE cellulose column chromatography, and sephadex G-100 gel filtration with a 4.0 purification fold. The molecular mass of the purified enzyme was estimated by SDS-PAGE to be 27 kDa. The optimal pH and temperature for the purified protease activity were 10.0 and $50^{\circ}C$, respectively. The purified enzyme was relatively stable at the pH range of 6.0-11.0 and at the temperature below $50^{\circ}C$. This enzyme was activated by $Ca^{2+}$ and $Mg^{2+}$ and inhibited by $Hg^{2+}$, $Cu^{2+}$, $Zn^{2+}$, $Al^{3+}$, $Ag^{2+}$. And this enzyme was strongly inhibited by PMSF, suggesting that it belongs to the serine protease superfamily.

Direct Divergence Approximation between Probability Distributions and Its Applications in Machine Learning

  • Sugiyama, Masashi;Liu, Song;du Plessis, Marthinus Christoffel;Yamanaka, Masao;Yamada, Makoto;Suzuki, Taiji;Kanamori, Takafumi
    • Journal of Computing Science and Engineering
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    • v.7 no.2
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    • pp.99-111
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    • 2013
  • Approximating a divergence between two probability distributions from their samples is a fundamental challenge in statistics, information theory, and machine learning. A divergence approximator can be used for various purposes, such as two-sample homogeneity testing, change-point detection, and class-balance estimation. Furthermore, an approximator of a divergence between the joint distribution and the product of marginals can be used for independence testing, which has a wide range of applications, including feature selection and extraction, clustering, object matching, independent component analysis, and causal direction estimation. In this paper, we review recent advances in divergence approximation. Our emphasis is that directly approximating the divergence without estimating probability distributions is more sensible than a naive two-step approach of first estimating probability distributions and then approximating the divergence. Furthermore, despite the overwhelming popularity of the Kullback-Leibler divergence as a divergence measure, we argue that alternatives such as the Pearson divergence, the relative Pearson divergence, and the $L^2$-distance are more useful in practice because of their computationally efficient approximability, high numerical stability, and superior robustness against outliers.

Thermostable Xylanase from Marasmius sp.: Purification and Characterization

  • Ratanachomsri, Ukrit;Sriprang, Rutchadaporn;Sornlek, Warasirin;Buaban, Benchaporn;Champreda, Verawat;Tanapongpipat, Sutipa;Eurwilaichitr, Lily
    • BMB Reports
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    • v.39 no.1
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    • pp.105-110
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    • 2006
  • We have screened 766 strains of fungi from the BIOTEC Culture Collection (BCC) for xylanases working in extreme pH and/or high temperature conditions, the so-called extreme xylanases. From a total number of 32 strains producing extreme xylanases, the strain BCC7928, identified by using the internal transcribed spacer (ITS) sequence of rRNA to be a Marasmius sp., was chosen for further characterization because of its high xylanolytic activity at temperature as high as $90^{\circ}C$. The crude enzyme possessed high thermostability and pH stability. Purification of this xylanase was carried out using an anion exchanger followed by hydrophobic interaction chromatography, yielding the enzyme with >90% homogeneity. The molecular mass of the enzyme was approximately 40 kDa. The purified enzyme retained broad working pH range of 4-8 and optimal temperature of $90^{\circ}C$. When using xylan from birchwood as substrate, it exhibits $K_m$ and $V_{max}$ values of $2.6{\pm}0.6\;mg/ml$ and $428{\pm}26\;U/mg$, respectively. The enzyme rapidly hydrolysed xylans from birchwood, beechwood, and exhibited lower activity on xylan from wheatbran, or celluloses from carboxymethylcellulose and Avicel. The purified enzyme was highly stable at temperature ranges from 50 to $70^{\circ}C$. It retained 84% of its maximal activity after incubation in standard buffer containing 1% xylan substrate at $70^{\circ}C$ for 3 h. This thermostable xylanase should therefore be useful for several industrial applications, such as agricultural, food and biofuel.

Study on Effect of Warmth Therapy Nursing Intervention Program after Laparoscopic Cholecystectomy (복강경담낭절제술 후 가온요법 간호중재 프로그램 적용 효과)

  • Lee, Jung-Geun
    • Journal of the Korea Academia-Industrial cooperation Society
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    • v.21 no.7
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    • pp.350-356
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    • 2020
  • Purpose: This study is a non-equilibrium control-like experimental study that attempts to develop a nursing intervention plan and to present basic data by grasping the effect of the heating therapy nursing intervention program on patients entering the recovery room after surgery. Method: The subjects of the study were 31 in an experimental group and 31 in a control group who applied one heating therapy program located in D city. The warming therapy was conducted in a recovery room in the range of 38 to 43℃ through a heater. The general characteristics of the subjects were determined by real number and percentage, and a homogeneity test between the experimental group and the control group was determined by 𝑥2-test and independent t-test. The difference in body temperature, pain, and tremor over time between the two groups was determined by repeated measure ANOVA. Results: First, the results of repeated measurements immediately after surgery showed significant differences in body temperature, pain, and tremor between the two groups. Second, temperature comfort showed a significant difference. Conclusion: The results confirmed that there was a positive effect on the patient in the intervention of warming therapy after surgery.

Purification and Characterization of Two Alkaline Proteases Produced by Pseudomonas sp. BK7

  • 이은구;박은희;현형환
    • Journal of Microbiology and Biotechnology
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    • v.10 no.5
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    • pp.667-667
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    • 2000
  • Pseudomonas sp. BK7, an alkalophile, displayed the highest growth and protease activity when grown in a fermenter which was controlled at a pH level of 9.0, and the enzyme production was significantly enganced by the increase of agitation speed. Two formas of alkaline proteases (BK7-1 and BK7-2) were fractionated and purified to near homogeneity. Protease BK7-1 was purified through CM-Sepharose CL-6B and Sephadex G-75 column chromatographies, and Protease BK7-2 was purified through CM-Sepharose CL-6B and Sephadex G-75 column chromatographies, and Protease BK7-2 was purified through CM-Sepharose CL-6B, DEAE-Sepharose, and Sephadex G-75 column chromatographies. The molecular weights of proteases BK7-1 and BK7-2 determined by gel filtration chromatography were 20,700 and 40,800, respectively. The $K_m$ value, isoelectric point, and optimum pH of protease BK7-1 were 2.55 mg/ml, 11.0 and 11.0, respectively, whereas those of protease BK7-2 were 1.57 mg/ml, 7.2, and 10.0, respectively. Both protease were practically stable in the pH range of 5-11. The optimum temperatures for the activities of both protease BK7-1 and BK7-2 were 50℃ and 45℃, respectively. About 56% of the original protease BK7-2 activity remained after being treated at 50℃ for 30 min but protease BK7-1 was rapidly inactivated at above 25℃. Both proteases were completely inhibited by phenylmethane sulfonyl fluoride, a serine protease inhibitor. Protease BK7-2 was stable against EDTA, EGTA, STP, and detergents such as SDS and LAS, whereas protease BK7-1 was found to be unstable.

Expression and Biochemical Characterization of Cold-Adapted Lipases from Antarctic Bacillus pumilus Strains

  • Litantra, Ribka;Lobionda, Stefani;Yim, Joung Han;Kim, Hyung Kwoun
    • Journal of Microbiology and Biotechnology
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    • v.23 no.9
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    • pp.1221-1228
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    • 2013
  • Two lipase genes (bpl1 and bpl3) from Antarctic Bacillus pumilus strains were expressed in Bacillus subtilis. Both recombinant lipases BPL1 and BPL2 were secreted to the culture medium and their activities reached 3.5 U/ml and 5.0 U/ml, respectively. Their molecular masses apparent using SDS-PAGE were 23 kDa for BPL1 and 19 kDa for BPL3. Both lipases were purified to homogeneity using ammonium sulfate precipitation and HiTrap SP FF column and Superose 12 column chromatographies. The final specific activities were estimated to be 328 U/mg for BPL1 and 310 U/mg for BPL3. Both lipases displayed an optimum temperature of $35^{\circ}C$, similar to other mesophilic enzymes. However, they maintained as much as 70% and 80% of the maximum activities at $10^{\circ}C$. Accordingly, their calculated activation energy at a temperature range of $10-35^{\circ}C$ was 5.32 kcal/mol for BPL1 and 4.26 kcal/mol for BPL3, typical of cold-adapted enzymes. The optimum pH of BPL1 and BPL3 was 8.5 and 8.0, respectively, and they were quite stable at pH 7.0-11.0, showing their strong alkaline tolerance. Both lipases had a preference toward medium chain length ($C_6-C_{10}$) fatty acid substrates. These results indicate the potential for the two Antarctic B. pumilus lipases as catalysts in bioorganic synthesis, food, and detergent industries.

Purification and Characterization of a Cyclohexanol Dehydrogenase from Rhodococcus sp. TK6

  • Kim, Tae-Kang;Choi, Jun-Ho;Rhee, In-Koo
    • Journal of Microbiology and Biotechnology
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    • v.12 no.1
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    • pp.39-45
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    • 2002
  • Activity staining on the native polyacrylamide gel electrophoresis (PAGE) of a cell-free extract of Rhodococcus sp. TK6, grown in media containing alcohols as the carbon source, revealed at least seven isozyme bands, which were identified as alcohol dehydrogenases that oxidize cyclohexanol to cyclohexanone. Among the alcohol dehydrogenases, cyclohexanol dehydrogenase II (CDH II), which is the major enzyme involved in the oxidation of cyclohexanol, was purified to homogeneity. The molecular mass of the CDH II was determined to be 60 kDa by gel filtration, while the molecular mass of each subunit was estimated to be 28 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The CDH II was unstable in acidic and basic pHs, and rapidly inactivated at temperatures above $40^{\circ}C$ . The CDH II activity was enhanced by the addition of divalent metal ions, like $Ba^2+\;and\;Mg^{2+}$. The purified enzyme catalyzed the oxidation of a broad range of alcohols, including cyclohexanol, trans-cyclohexane-1,2-diol, trans-cyclopentane-l,2-diol, cyclopentanol, and hexane-1,2-diol. The $K_m$ values of the CDH II for cyclohexanol, trans-cyclohexane-l,2-diol, cyclopentanol, trans-cyclopentane-l,2-diol, and hexane-l,2-diol were 1.7, 2.8, 14.2, 13.7, and 13.5 mM, respectively. The CDH II would appear to be a major alcohol dehydrogenase for the oxidation of cyclohexanol. The N-terminal sequence of the CDH II was determined to be TVAHVTGAARGIGRA. Furthermore, based on a comparison of the determined sequence with other short chain alcohol dehydrogenases, the purified CDH II was suggested to be a new enzyme.