• Title/Summary/Keyword: sodium azide

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Antimutagenicity of Phellinus linteus in Salmonella typhimurium

  • Shon, Yun-Hee;Lee, Jae-Sung;Lee, Hang-Woo;Kim, Joong-Wan;Lim, Jong-Kook;Kim, Cheorl-Ho;Nam, Kyung-Soo
    • Journal of Microbiology
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    • v.37 no.3
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    • pp.136-140
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    • 1999
  • The mutagenicities and antimutagenicities of butanol (PL I) and water (PL II) extracts from the filtrate of the cultured broth of Phellinus linteus were examined using the Ames/Salmonella test. No mutagenic activity of PL I and PL II was found in Salmonella typhimurium strains TA98 and TA100, either with or without S9 activation. In contrast, PL I and PL II showed inhibitory effects on the mutagenic activities induced by the directly-acting mutagens, 4-nitro-o-phenylenediamine (NPD) using the tester strain TA98 and sodium azide (NaN3) using the tester strain TA 100 in the absence of S9 mix. PLI and PL II also showed inhibitory effects on the mutagenicities of the indirectly-acting mutagens, 2-aminofluorene (2-AF) using the tester strain TA98 and benzo[a]pyrene (B[a]P) using the tester strain TA 100 in the presence of S9. These results suggest that P. linteus has an antimutagenic activity and may play a role in the prevention of cancer.

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Purification and Properties of Laccase of the White-rot Basidiomycete Coriolus hirsutus

  • Lee, Yeo-Jin;Shin, Kwang-Soo
    • Journal of Microbiology
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    • v.37 no.3
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    • pp.148-153
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    • 1999
  • Laccase produced by Coriolus hirsutus was purified to electrophoretic homogeneity by acetone precipitation, Sephacryl S-2000 HR chromatography, DEAE Sepharose CL-6B chromatography, and Mono Q HR 5/5 chromatography. The purification of laccase was 46.6-fold with an overall yield of 23.7%. Laccase from this fungus was a monomeric glycoprotein with 16% carbohydrate content, and has an isoelectric point of 4.2, and molecular mass of 78 kDa, respectively. The N-terminal amino acid sequence of the enzyme showed significant homology to hoste of laccases from Coriolus versicolor, Pycnoporus cinnabarius, and an unidentified basidiomycete, PM1. The highest rate of 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) oxidation by laccase was reached at 45$^{\circ}C$, and te pH optima of the enzyme varied depending on the substrate in the range of 2.0 to 4.5. The enzyme was stable at 60$^{\circ}C$ for 5 h and lost 80% activity at 80$^{\circ}C$ in 30 min. The enzyme oxidized a variety of usual laccase substrates including lignin-related phenol, and had the highest affinity toward ABTS. Under standard assay conditions, the apparent Km value of the enzyme toward ABTS was 8.1 ${\mu}$M. The enzyme was completely inhibited by L-cysteine and sodium azide, but not by potassium cyanide, SDS, ad thiourea.

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Chemical Modification of the Biodegradative Threonine Dehydratase from Serratia marcescens with Arginine and Lysine Modification Reagents

  • Choi, Byung-Bum;Kim, Soung-Soo
    • BMB Reports
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    • v.28 no.2
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    • pp.124-128
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    • 1995
  • Biodegradative threonine dehydratase purified from Serratia marcescens ATCC 25419 was inactivated by the arginine specific modification reagent, phenylglyoxal (PGO) and the lysine modification reagent, pyridoxal 5'-phosphate (PLP). The inactivation by PGO was protected by L-threonine and L-serine. The second order rate constant for the inactivation of the enzyme by PGO was calculated to be 136 $M^{-1}min^{-1}$. The reaction order with respect to PGO was 0.83. The inactivation of the enzyme by PGO was reversed upon addition of excess hydroxylamine. The inactivation of the enzyme by PLP was protected by L-threonine, L-serine, and a-aminobutyrate. The second order rate constant for the inactivation of the enzyme by PLP was 157 $M^{-1}min^{-1}$ and the order of reaction with respect to PLP was 1.0. The inactivation of the enzyme by PLP was reversed upon addition of excess acetic anhydride. Other chemical modification reagents such as N-ethylmaleimide, 5,5'-dithiobis (2-nitrobenzoate), iodoacetamide, sodium azide, phenylmethyl sulfonylfluoride and diethylpyrocarbonate had no effect on the enzyme activity. These results suggest that essential arginine and lysine residues may be located at or near the active site.

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Properties of Active Sites of Chitinase from Aerornonas salmonicida YA7-625 (Aeromonas salmonicida YA7-625가 생산하는 Chitinase의 활성부위 특성)

  • 이강표;최선진;오두환;문순옥
    • Microbiology and Biotechnology Letters
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    • v.20 no.1
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    • pp.68-72
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    • 1992
  • To investigate the characteristics of active sites of the chitinase isolated from AWOrnonus sulmonicidu YA7-625, effects of various chemicals un the enzyme activity were analyzed. $Hg^{2+}, Mn^[2+} \;and \; Cu^{2+}$ ' ions inhibited the activity of chitinase, while $Ca^{2+} , Zn^[2+} , Co^[2+} \; and\; Mg^[2+}$ ions at 1 mM stimulated enzyme activity. The chitinase was not inhibited by sulfhydryl ;gents, phenylglyoxal, and hydroxylamine, but was inhibited by iodine and N-bromosuccinimide. The $pK_{ps2} and pK_{ps2}$, values of chitinase were 4.04 a d 10.10, respectively. These results suggested that the chitinase from A~ronmzus salmonici& YA7-625 contains histidine, tyrosine. and tryptophan at the active center.

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Antimutagenic Activity and Cytotoxicity of the Whole Plant of Rumex acetosa (수영의 항돌연변이 활성 및 세포독성)

  • Lee, Nam-Jae;Lee, Kyung-Hee;Park, Sang-Shin;Han, Yeong-Hwan;Ryu, Shi-Yong;Lee, Dong-Ung
    • Korean Journal of Pharmacognosy
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    • v.32 no.4 s.127
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    • pp.338-343
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    • 2001
  • The extract and fractions of Rumex acetosa (Polygonaceae), a Korean medicinal plant, were examined for their cytotoxicities against five cultured human tumor cell lines, i.e. A549 (non-small cell lung), SK-OV-3 (ovary), SK-MEL-2 (melanoma), XF498 (central nerve system) and HCY15 (colon), using the SRB (sulforhodamine-B) method in vitro and antimutagenic activities by Ames test with Salmonella typhimurium TA98 and TA100 and SOS chromotest with E. coli PQ37. Among the tested samples, the methylene chloride fraction strongly inhibited the proliferation of each examined tumor cell line with $IC_{50}$ values ranged from 13.2 to $18.7\;{\mu}g/ml$ and showed potent antimutagenic activities with 96.1% and 96.7% at the concentration of 1 mg/plate against the mutagens, NPD and sodium azide, respectively. Its antigenotoxic activity was also very effective at the final concentration of $10\;{\mu}g/reaction$ tube against the mutagens, MNNG and NQO by SOS chromotest.

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Bacterial Reverse Mutation Test of CP pharmacopunture (세균을 이용한 CP 약침의 복귀돌연변이 시험)

  • Hwang, Ji Hye;Ku, Jaseung;Jung, Chul
    • The Journal of Korean Medicine
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    • v.41 no.3
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    • pp.55-65
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    • 2020
  • Objectives: This study aimed to evaluate the toxicity of CP pharmacopunture using bacterial reverse mutation test. Methods: To determine the mutagenic potential of CP pharmacopunture, histidine requiring Salmonella typhimurium (TA98, TA100, TA1535, and TA1537) and tryptophan requiring Escherichia coli (WP2uvrA, pKM101) strains were used. The negative (normal saline solution) and positive (Sodium azide, 2-Nitrofluorene, 2-Aminoanthracene, 9-Aminoacridine, and 4-Nitroquinoline N-oxide) control groups were used. To determine the dose levels of the main study, a dose range-finding study was conducted. Results: As a results of the dose range-finding study, the growth inhibition by CP pharmacopunture was not evident at any dose levels in the absence and presence of metabolic activation. As a results of the main study, the mean number of revertant colonies was less than twice when compared to the negative control values at all dose levels of the CP pharmacopuncture in the presence and absence of metabolic activation, showing no dose-related increase. In the positive control group, the number of revertant colonies was markedly increased by more than twice when compared to the negative control group. Conclusion: According to the results of this study, CP pharmacopunture did not show any signs of mutagenic potential.

The Dynamics of Protein Decomposition in Lakes of Different Trophic Status - Reflections on the Assessment of the Real Proteolytic Activity In Situ

  • Siuda, Waldemar;Kiersztyn, Bartosz;Chrost, Ryszard J.
    • Journal of Microbiology and Biotechnology
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    • v.17 no.6
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    • pp.897-904
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    • 2007
  • The aim of this paper is to discuss the methodology of our investigation of the dynamics of protein degradation and the total in situ protealytic activity in meso/eutrophic, eutrophic, and hypereutrophic freshwater environments. Analysis of the kinetics and rates of enzymatic release of amino acids in water samples preserved with sodium azide allows determination of the concentrations of labile proteins $(C_{LAB})$, and their half-life time $(T_{1/2})$. Moreover, it gives more realistic information on resultant activity in situ $(V_{T1/2})$ of ecto- and extracellular proteases that are responsible for the biological degradation of these compounds. Although the results provided by the proposed method are general y well correlated with those obtained by classical procedures, they better characterize the dynamics of protein degradation processes, especially in eutrophic or hypereutrophic lakes. In these environments, processes of protein decomposition occur mainly on the particles and depend primarily on a metabolic activity of seston-attached bacteria. The method was tested in three lakes. The different degree of eutrophication of these lakes was clearly demonstrated by the measured real proteolytic pattern and confirmed by conventional trophic state determinants.

Selective Inhibition of Ammonia Oxidation and Nitrite Oxidation Linked to $N_2O$ Emission with Activated Sludge and Enriched Nitrifiers

  • Ali, Toor Umair;Kim, Minwook;Kim, Dong-Jin
    • Journal of Microbiology and Biotechnology
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    • v.23 no.5
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    • pp.719-723
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    • 2013
  • Nitrification in wastewater treatment emits a significant amount of nitrous oxide ($N_2O$), which is one of the major greenhouse gases. However, the actual mechanism or metabolic pathway is still largely unknown. Selective nitrification inhibitors were used to determine the nitrification steps responsible for $N_2O$ emission with activated sludge and enriched nitrifiers. Allylthiourea (86 ${\mu}M$) completely inhibited ammonia oxidation and $N_2O$ emission both in activated sludge and enriched nitrifiers. Sodium azide (24 ${\mu}M$) selectively inhibited nitrite oxidation and it led to more $N_2O$ emission than the control experiment both in activated sludge and enriched nitrifiers. The inhibition tests showed that $N_2O$ emission was mainly related to the activity of ammonia oxidizers in aerobic condition, and the inhibition of ammonia monooxygenase completely blocked $N_2O$ emission. On the other hand, $N_2O$ emission increased significantly as the nitrogen flux from nitrite to nitrate was blocked by the selective inhibition of nitrite oxidation.

Characteristic as a Gene Delivery System of Water Soluble Chitosan Conjugated with Cationic Peptide (양이온 펩타이드가 컨쥬게이트된 수용성 키토산의 유전자 전달체로서의 특성)

  • Kim, Young-Min;Kim, Ji-Ho;Park, Seong-Cheol;Park, Yung-Hoon;Jang, Mi-Kyeong
    • KSBB Journal
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    • v.31 no.4
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    • pp.300-311
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    • 2016
  • Recently gene delivery has been designed newly using bioactive biomaterial and applied in the various field by many researchers. In this study, we proposed a new gene delivery system which has the capability of targeting effect in the specific tissue and remarkably enhanced transfection efficiency. We investigated $^1H-NMR$ spectroscopy, particle size analyzer and gel retardation to confirm the correct preparation of gene delivery. Also, we identified the hemo-compatibility of gene delivery by hemolysis assay, non-cytotoxicity by MTT test and transfection efficiency. The uptake mechanism of the gene carrier was confirmed using inhibitor agent such as sodium azide, indomethacin, quercetin, colchicine, and chloropromazine. As a results, it was identified that gene carrier prepared by in this study entered in the cell by the microtubule-dependent, energy-dependent and clathrin-mediated endocytosis pathway.

A New Adamantane-like Tetranuclear Manganese(III) Complex Based on Flexible Schiff-base Ligand: Synthesis, Crystal Structure and Magnetic Property

  • Zhang, Ran;Ni, Zhong-Hai;Zhang, Li-Fang;Kou, Hui-Zhong
    • Bulletin of the Korean Chemical Society
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    • v.35 no.7
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    • pp.1965-1969
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    • 2014
  • A new tetranuclear Mn(III) complex $[Mn^{III}{_4}(sae)_4({\mu}_3-O)({\mu}_{1,1}-N_3)(OH)(H_2O)_2]{\cdot}H_2O$ (1) ($H_2sae$ = 2-salicylideneamino-1-ethanol) has been synthesized by the reaction of $MnCl_2{\cdot}4H_2O$, $H_2sae$ and sodium azide in the mixed solvent of methanol, acetonitrile and water. The X-ray diffraction analysis shows that the four Mn(III) ions in complex 1 have a unique adamantine arrangement, whereas the coordination environment of each Mn(III) ions is different. Magnetic studies indicate that complex 1 manifests antiferromagnetic behaviors. The magnetic susceptibilities of complex 1 have been fitted by two magnetic models based on the suitable analysis of its magnetic structural topology.