• Title/Summary/Keyword: D-adenosine

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Actinomycins에 의한 Adenosine Deaminase의 억제

  • 김경자;조성진
    • Microbiology and Biotechnology Letters
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    • v.24 no.3
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    • pp.380-383
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    • 1996
  • Adenosine deaminase inhibitor was extracted from culture broth of Streptomyces sp. strain V-8 with ethylacetate. The ethylacetate extract showed the characteristic UV absorption spectrum of actinomycins at 440-450 nm. The ethylacetate extract was compared with respect to inhibitory behavior against adenosine deaminase from calf intestinal mucosa with actinomycin D, -C complex and actinomycin V. The Ki values for actnomycin D, -C complex, and actinomycin V against adenosine deaminase were determined to be 9.9 $\times$ 10$^{-6}$ M, 9.6 $\times$ 10$^{-6}$ M and 9.3 $\times$ 10$^{-6}$ M, respectively. The Ki value for the ethylacetate extract of culture broth against adenosine deaminase was determined to be 5.7 $\times$ 10$^{-6}$ M. The kinetic parameters of actinomycin D, -C complex, -V and ethylacetate extract of culture broth for adenosine deaminase were as follows:I$_{50}$ = 1.5 $\times$ 10$^{-5}$ M (actinomycin D), 2.7 $\times$ 10$^{-5}$ M (actinomycin C complex), 3.5 $\times$ 10$^{-5}$ M (actinomycin V), 8.9 $\times$ 10$^{-6}$ M (ethylacetate extract of culture broth). The adenosine deaminase was inhibited noncompetitively by ethylacetate extract of culture broth as well as by actinomycin D, -C complex and actinomycin V.

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Visible and Fast Assay System for Tobacco Transformant Introduced with Adenosine Deaminase Marker Gene (Adenosine Deaminase 표지유전자로 형질전환된 연초의 신속한 Assay 방법)

  • 양덕춘;김용환;임학태;방극수;배창휴
    • Korean Journal of Plant Tissue Culture
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    • v.28 no.3
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    • pp.165-171
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    • 2001
  • New visible and fast assay system have been developed for tobacco transformant introduced with adenosine deaminase (ADA) marker gene, which converts cytotoxic adenosine analogues to non-toxic inosine analogues and ammonia. Ammonia was changed to blue color in the solution of phenol-nitoprusside and alkaline-hypochlorite. It was possible to detect activity of ADA visibly on the holes of 96 well plate using tiny explant of transgenic tobacco leaves within 1 hour incubation time. As substrates of ADA enzyme from transgenic plant on the plate, a number of adenosine analogues such as 9-D-arabinofuranosyl adenine, cordycepin, 2'-deoxyadenosine, adenosine and xylofuranosyl adenine were possible for detection of ADA activity. Optimal condition of substrate for ADA enzyme was each 10 mM and pH 7.5 in adenosine solution. Especially, transgenic plant did not convert adenosine to inosine and ammonia in the presence of ADA inhibitor deoxycoformycin, which means that ammonia produced from transgenic plant is due to expression of ADA gene. Now, we show that this detection system can be easily, sensitively, fast and cheaply as well as visibly assayed in vitro as GUS gene system with very small size of transformant explant.

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Adenosine Deaminase Gene: Possible Selectable Marker for Tobacco Transformation (연초의 형질전환을 위한 새로운 표지유전자로서 Mouse Adenosine Deaminase 유전자의 이용가능성)

  • 양덕춘;한성수;윤의수
    • Korean Journal of Plant Tissue Culture
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    • v.22 no.4
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    • pp.235-240
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    • 1995
  • The development of selectable markers for transformation has been a major factor in the successful genetic manipulation of plant. We established a new selectable marker system for tobacco transformation using chimeric adenosine deaminase (ADA) gene, which confers resistance to cytotoxic adenosine analogues, 9-$\beta$-D-arabinofuranosyl adenine(Ara-A) and cordycepin. The transformants with the chimeric ADA gene in tobacco grew in the presence of normally lethal level of cytotoxic adenosine analogues, 100 $\mu$M Ara-A and 50 $\mu$M cordycepin. We successfully distinguished transformed shoot from non-transformed shoot on the same selectable media with cytotoxic adenosine analogues. In this selectable media, we were able to select seeds with/ without ADA gene from transgenic tobacco seeds. Theses results show that the mammalian ADA gene may serve as a new selectable marker for tobacco transformation.

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Effect of Cholera Toxin, Dibutyryl cAMP and Adenosine on the In Vitro Reactivation of Latent Herpes Simplex Virus

  • Cheong, D.K.;Park, N.H.
    • Toxicological Research
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    • v.4 no.1
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    • pp.47-53
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    • 1988
  • Cholera toxin and dibutyryl cyclic adenosine 3', 5'-monophosphate(db-cAMP) increased the rate and number of infections units produced in the in vitro reactivation of latent herpes simplex virus, whereas adenosine diminished them. cAMP concentration in latently infected trigeminal ganglia of mice was greatly increased by cholera toxin but was not affected by adenosine.

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Chemical Constituents of the Sclerotia of Grifola umbellata (저령(Grifola umbellata)균핵의 추출성분)

  • 이학주;이경태;박영기;이민웅
    • Journal of Korea Foresty Energy
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    • v.21 no.1
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    • pp.16-24
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    • 2002
  • Three alkaloids and two steroids were isolated from the sclerotia of Grifola umbellata. Structures of the isolated compounds were determined as 9-$\beta$-D-ribofuranosyladenine (adenosine), 1-$\beta$-D-ribofuranosyluracil (uridine), 2,4-pyrimidinedione (uracil), ergosta-4, 6, 8 (14), 22-tetraen-3-one and ergosta-5, 7, 22-tritene-$3\beta$-ol (ergosterol) respectively on the basis of spectroscopic data and chemical correlations.

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Chemical Constituents from the Fruit Bodies of Lentinula edodes (표고(Lentinula edodes) 자실체의 추출성분)

  • Lee, Hak-Ju;Yoon, Kab-Hee;Bak, Won-Chull
    • Journal of the Korean Wood Science and Technology
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    • v.31 no.2
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    • pp.24-30
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    • 2003
  • Three nucleotides, one amide, acid and steroid, were isolated from the fruit bodies of Lentinula edodes. The structures were determined as adenosine (9-𝛽-D-ribofuranosyladenine), uridine (1-𝛽-D-ribofuranosyluracil), uracil (2, 4-pyrimidinedione), nicotinamide, p-hydroxybenzoic acid and ergosterol (ergosta-5, 7, 22-triene-3𝛽-ol), respectively, on the basis of spectroscopic data and chemical correlations.

Coumarin Glycosides from the Roots of Angelica dahurica

  • Kim, Seoung-Han;Kang, Sam-Sik;Kim, Chang-Min
    • Archives of Pharmacal Research
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    • v.15 no.1
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    • pp.73-77
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    • 1992
  • From the roots of Angelica dahurica Bentham et Hooker (Umbelliferae), five coumarin glucosides together with adenosine have been isolated and identified as nodakenin, 3'-hydroxymarmesinin, tert-O-$\beta$-D-glucopyranosyl-byakangelicin, sec-O-$\beta$-D-glucopyranosyl-byakangelicin and scopolin. This is the first report of the occurrence of these compounds in this plant.

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The Effects of Intravenous Adenosine Infusion on Intraoperative Remifentanil Requirements and Postoperative Pain in Elective Tonsillectomies Are Influenced by the Time of Day the Operation Is Performed (일 중 수술시간이 다른 편도절제술에서 Adenosine 정주가 술 중 Remifentanil 요구량과 수술 후 통증에 미치는 영향)

  • Lee, Cheol;Lee, Kyu Chang;Kim, Hye Young;Bahn, Jong Min;Choi, Eun Kyung;Lee, Myeong Jong
    • The Korean Journal of Pain
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    • v.22 no.2
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    • pp.135-140
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    • 2009
  • Background: The chronobiology of postoperative pain is an interesting topic. This study was performed to evaluate the effects of adenosine on inta-operative remifentanil requirements and on postoperative pain in patients undergoing tonsillectomies and how those effects change with changing time of day the surgery is performed. Methods: For this study, 120 patients were randomly allocated into four groups. Patients in groups B and D received adenosine at a dose of $50{\mu}g/kg/min$, and those in group A and C received an equal volume of saline from 10 minutes after the induction of anesthesia until the end of surgery. Group A (saline) and B (adenosine) patients entered the operating room after 08:30 and finished before 11:00, Group C (saline) and D (adenosine) patients entered the operating room after 13:30 and finished before 16:00. We evaluated the intraoperative time-weighted mean remifentanil dose, and postoperative pain scores at 1, 6, 12, and 24 hours, and the analgesic dose required during the following 24 hours. Results: Time-weighted mean remifentanil doses during the intraoperative period and the analgesic requirement during the following 24 hours in group D was significantly lower than in the other groups. The numeric rating scale for pain at 1, and 6 hours in group D was significantly lower (P < 0.01) than that of group A. There were no significant differences in side effects among groups. Conclusions: Use of intraoperative adenosine infusion provides perioperative analgesia. Postoperative pain is affected by the time of day the operation is performed.

Synthesis and Binding Affinity of Homologated Adenosine Analogues as A3 Adenosine Receptor Ligands

  • Lee, Hyuk-Woo;Choi, Won-Jun;Jacobson, Kenneth A.;Jeong, Lak-Shin
    • Bulletin of the Korean Chemical Society
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    • v.32 no.5
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    • pp.1620-1624
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    • 2011
  • Homologated analogues 3a and 3b of potent and selective A3 adenosine receptor ligands, IB-MECA and dimethyl-IB-MECA were synthesized from commercially available 1-O-acetyl-2,3,5-tri-O-benzoyl-${\beta}$-D-ribofuranose (4) via $Co_2(CO)_8$-catalyzed siloxymethylation as a key step. Unfortunately, homologated analogues 3a and 3b did not show significant binding affinities at three subtypes of adenosine receptors, indicating that free rotation, resulting from homologation, induced unfavorable interactions in the binding site of the receptor maybe due to the presence of many conformations.

Enzymatic Properties of Intracellular Adenosine Deaminase from Nocardioides sp. J-326TK

  • Hong-Ki Jun;Tae-Sook Kim
    • Journal of Life Science
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    • v.9 no.1
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    • pp.64-68
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    • 1999
  • The properties of purified intracellular adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4) of Nocardioides sp. J-326TK isolated from soil have been studied. The enzyme deaminated adenosine and 2`-deoxyadenosine and the respective {TEX}$K_{M}${/TEX} values were 4.0×{TEX}$10^{-4}${/TEX} M and 5.0× {TEX}$10^{-4}${/TEX} M, but the enzyme was not active on 8-bromoadenosine, 6-methylaminopurine riboside, ATP, ADP, 2`-AMP, 3`-AMP, 5`-AMP, dAMP, cAMP, NAD, FAD, NADP and adenine. The enzyme activity was strongly inhibited by the addition of {TEX}$Hg^{2+}${/TEX} and {TEX}$Ag^{+}${/TEX}, {TEX}$Cu^{2+}${/TEX}, {TEX}$Co^{2+}${/TEX} and {TEX}$Mn^{2+}${/TEX} also inhibited the activity but much less extent. The effect of alkyl reagents, metal chelating reagents and certain other compounds on the enzyme activity were also examined. No reagent activated the enzyme. On the contrary, the enzyme reaction was slightly inhibited by o-phenanthroline and 6-benzyladenosine.

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