• Title/Summary/Keyword: Adenine

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DNA-functionalized single-walled carbon nanotube-based sensor array for gas monitoring

  • Zhang, Wenjun;Liu, Yu;Wang, Ming. L
    • Smart Structures and Systems
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    • v.12 no.1
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    • pp.73-95
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    • 2013
  • Nine deoxyribonucleic acid (DNA) sequences were used to functionalize single-walled carbon nanotube (SWNT) sensors to detect the trace amount of methanol, acetone, and HCl in vapor. DNA 24 Ma (24 randomly arranged nitrogenous bases with one amine at each end of it) decorated SWNT sensor and DNA 24 A (only adenine (A) base with a length of 24) decorated SWNT sensor have demonstrated the largest sensing responses towards acetone and HCl, respectively. On the other hand, for the DNA GT decorated SWNT sensors with different sequence lengths, the optimum DNA sequence length for acetone and HCl sensing is 32 and 8, separately. The detection of methanol, acetone, and HCl have identified that DNA functionalized SWNT sensors exhibit great selectivity, sensitivity, and repeatability with an accuracy of more than 90%. Further, a sensor array composed of SWNT functionalized with various DNA sequences was utilized to identify acetone and HCl through pattern recognition. The sensor array is a combination of four different DNA functionalized SWNT sensors and two bare SWNT sensors (work as reference). This wireless sensing system has enabled real-time gas monitoring and air quality assurance for safety and security.

In vitro Propagation and Ex vitro Rooting of Tectona grandis (L.f ), APNBV-1 Clone

  • Ramesh, Kommalapati;Chandra, Mouli Kalla;Vijaya, Tartte
    • Journal of Forest and Environmental Science
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    • v.25 no.2
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    • pp.119-126
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    • 2009
  • An efficient in vitro plant regeneration system was developed through shoot proliferation from axillary buds of Tectona grandis (L.f), APNBV-1 (Andhra Pradesh North Badrachalam Venkatapuram-1) clone. Multiple shoots of high quality were produced in vitro from axillary bud explants. An average of 4.39 shoots/explant were obtained on Murashige and Skoog's (MS) medium supplemented with plant growth regulators (PGRs) benzyl amino purine (BA), kinetin (KN), indole acetic acid (IAA), gibberillic acid ($GA_3$), growth adjuvants casein hydrolysate (CH), adenine sulphate (Ads) and antioxidants ascorbic acid, polyvinyl pyrrollidine (PVP). Eighty five percent of rooting was observed in ex vitro rooting media containing IBA and vermiculite. In ex vitro rooting, single shoots with 2 to 3 nodes were subjected to IBA of different concentrations at different periods of time intervals. Direct rooting in vermiculite at 500 ppm concentration of IBA resulted in 4.3 number of roots with 2 cm length. Minimum response of rooting and length of roots were recorded at 100 ppm concentration of IBA. Planlets were transferred to plastic bags for short acclimatization stage in green house where they survived at 95%.

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Complex Formation of Adenosine 3',5'-Cyclic Monophosphate with β-Cyclodextrin: Kinetics and Mechanism by Ultrasonic Relaxation

  • Bae, Jong-Rim;Kim, Jeong-Koo;Lee, Chang-Woo
    • Bulletin of the Korean Chemical Society
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    • v.31 no.2
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    • pp.442-446
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    • 2010
  • Adenosine 3',5'-cyclic monophosphate (cAMP) is a second messenger responsible for a multitude of cellular responses. In this study, we utilized $\beta$-cyclodextrin ($\beta$-CD) as an artificial receptor with a hydrophobic cavity to elucidate the inclusion kinetics of cAMP in a hydrophobic environment using the ultrasonic relaxation method. The results revealed that the interaction of cAMP with $\beta$-CD followed a single relaxation curve as a result of host-guest interactions. The inclusion of cAMP into the $\beta$-CD cavity was found to be a diffusion-controlled reaction. The dissociation of cAMP from the $\beta$-CD cavity was slower than that of adenosine 5'-monophosphate (AMP). The syn and anti glycosyl conformations of adenine nucleotides are considered to play an important role in formation of the inclusion complex. Taken together, our findings indicate that hydrophobic interactions are involved in the inclusion complex formation of cAMP with $\beta$-CD and provide insight into the interactions of cAMP with cAMP-binding proteins.

Acupoint combination-related changes of NADPH-d diaphorase and neuronal nitric oxide synthase in the brainstem and cerebellum of spontaneously hypertensive rats (족삼리(足三里) 경혈배합(經穴配合)에 따른 SHR의 뇌줄기, 소뇌(小腦) 영역(領域)에서 NADPH-diaphorase와 nNOS, 신경세포(神經細胞)의 변화연구(變化硏究))

  • Lee, Hong-min;Kim, Chang-hwan;Kim, Yong-suk
    • Journal of Acupuncture Research
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    • v.20 no.6
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    • pp.148-159
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    • 2003
  • Objective: This study examines the effects of acupoint combination on NADPH-diaphorase and neuronal nitric oxide synthase(nNOS) in the brainstem of spontaneously hypertensive rats. Methods: The changes of NADPH-d-positive neurons using a histochemical method and the changes of nNOS-positive neurons using an immunohistochemical method were evaluated. The optical densities of NADPH-d-positive neurons and nNOS-positive neurons of the Choksamni(ST36) Umnungchon(SP9) groups were significantly increased in all brainstem areas as compared to the Choksamni and Choksamni Kokchi(LI11) groups and decreased, with the exeption of the nNOS-positive neurons in the superficial gray of superior colliculus, as compared to the normal group. Results: Our results demonstrated that electroacupuncture changes the activity in the NO system in the brainstem of SHR and the acupoint combination is one of the important parameters for this effect.

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Kinetic Mechanism of Nucleotide Binding to Escherichia coli Transcription Termination Factor Rho: Stopped-flow Kinetic Studies Using ATP and Fluorescent ATP Analogues

  • Kim, Dong-Eun
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.9 no.1
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    • pp.23-34
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    • 2004
  • Escherichia coli transcription termination factor Rho catalyzes the unwinding of RNA/DNA duplex in reactions that are coupled to ATP binding and hydrolysis. Fluorescence stopped-flow methods using ATP and the fluorescent 2'(3')-O-( N-methylanthraniloyl) derivatives (mant-derivatives) of ATP and ADP were used to probe the kinetics of nucleotide binding to and dissociation from the Rho-RNA complex. Presteady state nucleotide binding kinetics provides evidence for the presence of negative cooperativity in nucleotide binding among the multiple nucleotide binding sites on Rho hexamer. The binding of the first nucleotide to the Rho-RNA complex occurs at a bimolecular rate of 3.6${\times}$10$\^$6/ M$\^$-1/ sec$\^$-1/ whereas the second nucleotide binds at a slower rate of 4.7${\times}$10$\^$5/ M$\^$-1/ sec$\^$-1/ at 18$^{\circ}C$, RNA complexed with Rho affects the kinetics of nucleotide interaction with the active sites through conformational changes to the Rho hexamer, allowing the incoming nucleotide to be more accessible to the sites. Adenine nucleotide binding and dissociation is more favorable when RNA is bound to Rho, whereas ATP binding and dissociation step in the absence of RNA occurs significantly slower, at a rate ∼70- and ∼40-fold slower than those observed with the Rho-RNA complex, respectively.

Formate Decarboxylation: Initial Step for Hydrogen Production by Enterobacter aerogenes (Enterobacter aerogenes에 의한 수소 생산 초기 단계인 포메이트 탈카복시 반응 연구)

  • Choi, Jinyoung;Jho, Young Choong;Ahn, Ik-Sung
    • Applied Chemistry for Engineering
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    • v.20 no.4
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    • pp.449-452
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    • 2009
  • The absence of Fe, Se, and Mo in a minimal medium prevented the production of hydrogen from the anaerobic culture of Escherichia coli MC4100. Fe, Se, and Mo are known to be cofactors of formate dehydrogenase ($FDH_{II}$) of both E. coli and Enterobacter aerogenes. Hence when these trace elements are absent in the minimal medium, hydrogen production through formate dehydrogenation would be inhibited not only in E. coli but also in E. aerogenes. Hydrogen production by E. aerogenes 413 was delayed when lacking these trace elements. Therefore, it is believed that hydrogen production of E. aerogenes is initiated not by the reoxidation of nicotinamide adenine dinucleotide (NADH) but by formate decarboxylation.

The Expressional Changes of Nitric Oxide Synthase in the Rat Brain Following Food Restriction

  • Kang Kyounglan;Huh Youngbuhm;Park Chan;Choue Ryo Won
    • Nutritional Sciences
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    • v.8 no.4
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    • pp.231-236
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    • 2005
  • This study investigated the changes in the neuronal nitric oxide synthase (nNOS) and nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) activities during food restriction in the rat brain such as cerebral cortex, cerebellum, caudate pautamen and hypothalamus. The rats were placed on a restricted feeding schedule consisting of half the ad libitum quantity for 3 days and 1, 2, 4, 6 and 9 weeks, and a free feeding schedule for 4 weeks. The loss of body weight peaked after 1 week of food restriction and persisted during the entire 9-week period of food restriction. The dramatic weight change in the first week ($12\%$) and the reduction in weight changes thereafter suggest that major adaptation changes occur early and body maintenance occurs subsequently. In the hypothalamus, the optical densities of the NADPH-d and nNOS immunoreactivities were found to be significantly higher in the 1-week and lower in the 9-week food restricted group than in the ad libitum fed control rats. In contrast, in the cerebral cortex, the optical densities of the NADPH-d- and nNOS-positive neurons were not changed significantly during the period of food restriction. This study provides the morphological evidence showing that food restriction has a significant effect on the nitric oxide synthesizing system of the hypothalamus.

A New Assay Method for Spermidine and Spermine Synthases Using Antibody Against MTA

  • Lee, Sung-Ho;Cho, Young-Dong
    • BMB Reports
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    • v.30 no.6
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    • pp.443-447
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    • 1997
  • We have developed a novel method for assays of spermidine and spermine synthase (aminopropyltransferase) activities using antibody against 5'-deoxy-5'-methylthioadenosine (MTA). A new assay is reported here which is based on the observation that MTA is formed as a stoichiometric by-product of the spermidine and spermine synthases reactions. In order to determine MTA, a radioimmunoassay method with sensitivity and rapidity was used. (Lee and Cho, 1997). In this assay, adenine must be added in the reaction mixture, since it effectively inhibits the action of MTA phosphorylase by which MTA is metabolized. This assay is a improvement in term of sensitivity and time saving, compared to the currently used methods. It has a level of sensitivity (100 fmol) sufficient to monitor aminopropyltransferase activities in incubations containing as little as $10{\mu}g$ protein prepared from rat tissue homogenate. The results obtained showed that this method is particularly useful for cultured cells with low enzyme concentration. Moreover, this assay has the advantage which allows studies using alternative substrates (other amines). Spermidine synthase activity was high in rat liver, but low in rat kidney. The activity of spermine synthase was in most rat tissues very low as compared to that of spermidine synthase, but was high in brain.

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Purification and Properties of Alcohol Oxidase Produced by Hnasenula sp. MS-364 (Hansenula sp. MS-364가 생산하는 Alcohol Oxidase 의 정제 및 성질)

  • 김병호;김형만;권태종
    • Microbiology and Biotechnology Letters
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    • v.23 no.1
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    • pp.60-67
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    • 1995
  • Methanol assimilating yeast, Hansenula sp. MS-364 that has high productivity with methanol as carbon and energy source has been preserved at dept. of Microbiological engineering. Purification and properties of alcohol oxidase (E.C.1.1.3.13: oxygen oxidoreductase) were investigated in the methanol assimilating yeast, Hansenula sp. MS-364. Alcohol oxidase is related to the catalytic reaction that degrades alcohol to aldehyde and peroxide. The methanol oxidizing enzyme was purified by ammonium sulfate precipitation, DEAE-Sephadex A-50 chromatography and gel filtration on Sepharose 6B from cell-free extract. The purified enzyme preparation gave a single band in the sodium dodesyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight of the enzyme was calculated to be about 576,000 and molecular weight of subunit was also calculated to be 72,000. The optimal pH and temperature of the enzyme reaction were pH 7.5 and 37$\circ$C, respectively. The enzyme was unstable in acidic pH and higher temperature. The enzyme was not specific for methanol and also oxidized lower primary alcohols. The Km value for methanol was 2.5 mM and that for ethanol was 1.66 mM. The enzyme was heavily inhibited by metal ions such as Hg$^{2+}$, Ag$^{2+}$, Cu$^{2+}$. The high concentration of EDTA and sulfhydryl reagents strongly inhibited the enzyme activity. The component of coenzyme was determined to flavin adenine dinucleotide.

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Identification of the Phenalamide Biosynthetic Gene Cluster in Myxococcus stipitatus DSM 14675

  • Park, Suhyun;Hyun, Hyesook;Lee, Jong Suk;Cho, Kyungyun
    • Journal of Microbiology and Biotechnology
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    • v.26 no.9
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    • pp.1636-1642
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    • 2016
  • Phenalamide is a bioactive secondary metabolite produced by Myxococcus stipitatus. We identified a 56 kb phenalamide biosynthetic gene cluster from M. stipitatus DSM 14675 by genomic sequence analysis and mutational analysis. The cluster is comprised of 12 genes (MYSTI_04318- MYSTI_04329) encoding three pyruvate dehydrogenase subunits, eight polyketide synthase modules, a non-ribosomal peptide synthase module, a hypothetical protein, and a putative flavin adenine dinucleotide-binding protein. Disruption of the MYSTI_04324 or MYSTI_04325 genes by plasmid insertion resulted in a defect in phenalamide production. The organization of the phenalamide biosynthetic modules encoded by the fifth to tenth genes (MYSTI_04320-MYSTI_04325) was very similar to that of the myxalamid biosynthetic gene cluster from Stigmatella aurantiaca Sg a15, as expected from similar backbone structures of the two substances. However, the loading module and the first extension module of the phenalamide synthase encoded by the first to fourth genes (MYSTI_04326-MYSTI_04329) were found only in the phenalamide biosynthetic gene cluster from M. stipitatus DSM 14675.