About: Preparation of 1,2-disubstituted-3-hydroxy-4(1H)-quinolinones and the influence of substitution on the Course of Cyclization     Goto   Sponge   NotDistinct   Permalink

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  • Crude extract of Aspergillus niger AKU 3302 mycelia incubated with methylamine showed a single amine oxidase activity band in a developed polyacrylamide gel that weakly cross-reacted with the antibody against a copper/topa quinone-containing amine oxidase (AO-II) from the same strain induced by n-butylamine. Since the organism cannot grow on methylamine and the already known quinoprotein amine oxidases of the organism cannot catalyze oxidation of methylamine, the organism was forced to produce another enzyme that could oxidize methylamine when the mycelia were incubated with methylamine. The enzyme was separated and purified from the already known two quinoprotein amine oxidases formed in the same mycelia. The purified enzyme showed a sharp symmetric sedimentation peak in analytical ultracentrifugation showing S-20,w(0) of 6.5s, The molecular mass of 133 kDa estimated by gel chromatography and 66.6 kDa found by SDS-PAGE confirmed the dimeric structure of the enzyme. The purified enzyme was pink in col
  • Crude extract of Aspergillus niger AKU 3302 mycelia incubated with methylamine showed a single amine oxidase activity band in a developed polyacrylamide gel that weakly cross-reacted with the antibody against a copper/topa quinone-containing amine oxidase (AO-II) from the same strain induced by n-butylamine. Since the organism cannot grow on methylamine and the already known quinoprotein amine oxidases of the organism cannot catalyze oxidation of methylamine, the organism was forced to produce another enzyme that could oxidize methylamine when the mycelia were incubated with methylamine. The enzyme was separated and purified from the already known two quinoprotein amine oxidases formed in the same mycelia. The purified enzyme showed a sharp symmetric sedimentation peak in analytical ultracentrifugation showing S-20,w(0) of 6.5s, The molecular mass of 133 kDa estimated by gel chromatography and 66.6 kDa found by SDS-PAGE confirmed the dimeric structure of the enzyme. The purified enzyme was pink in col (en)
Title
  • Preparation of 1,2-disubstituted-3-hydroxy-4(1H)-quinolinones and the influence of substitution on the Course of Cyclization
  • Preparation of 1,2-disubstituted-3-hydroxy-4(1H)-quinolinones and the influence of substitution on the Course of Cyclization (en)
skos:prefLabel
  • Preparation of 1,2-disubstituted-3-hydroxy-4(1H)-quinolinones and the influence of substitution on the Course of Cyclization
  • Preparation of 1,2-disubstituted-3-hydroxy-4(1H)-quinolinones and the influence of substitution on the Course of Cyclization (en)
skos:notation
  • RIV/61989592:15310/99:00000788!RIV/2000/MSM/153100
http://linked.open.../vavai/riv/strany
  • 141
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(VS96021), Z(MSM 153100013)
http://linked.open...iv/cisloPeriodika
  • 1
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
  • Hlaváč, Jan
  • Lemr, Karel
http://linked.open.../riv/druhVysledku
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  • 750809
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  • RIV/61989592:15310/99:00000788
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http://linked.open...ontrolniKodProRIV
  • [DF151FE434FB]
http://linked.open...i/riv/nazevZdroje
  • JOURNAL OF HETEROCYCLIC CHEMISTRY
http://linked.open...in/vavai/riv/obor
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http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 36
http://linked.open...iv/tvurceVysledku
  • Hlaváč, Jan
  • Lemr, Karel
  • Hradil, P.
http://linked.open...n/vavai/riv/zamer
issn
  • 0022-152X
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http://localhost/t...ganizacniJednotka
  • 15310
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