| Attributes | Values |
|---|
| rdf:type
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| Description
| - Mycelia plísně Aspergillus niger AKU 3302 inkubovaná s methylaminem produkují enzym methylaminoxidasu, který přísluší k chinoproteinům. Enzym byl izolován chromatografickými metodami a byly určeny jeho vlastnosti. Jedná se o dimer (2 x 67 kDa), který je zbarven růžově díky přítomnosti chinonového kofaktoru. Methylaminoxidasa ochotně oxiduje methylamin, n-hexylamin a n-butylamin, nepůsobí na benzylamin, histamin a tyramin. Je inaktivována karbonylovými činidly a činidly chelatujícími dvojmocnou měď. Přítomnost kofaktoru topachinonu byla prokázána spektroskopickými metodami. Pomocí hmotnostní spektrometrie byla získána data o částečné aminokyselinové sekvenci enzymu. (cs)
- 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)
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| Title
| - Purifikace a charakterizace methylaminoxidasy indukované v Aspergillus niger AKU 3302 (cs)
- Purification and characterization of methylamine oxidase induced in Aspergillus niger AKU 3302
- Purification and characterization of methylamine oxidase induced in Aspergillus niger AKU 3302 (en)
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| skos:prefLabel
| - Purifikace a charakterizace methylaminoxidasy indukované v Aspergillus niger AKU 3302 (cs)
- Purification and characterization of methylamine oxidase induced in Aspergillus niger AKU 3302
- Purification and characterization of methylamine oxidase induced in Aspergillus niger AKU 3302 (en)
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| skos:notation
| - RIV/61989592:15310/99:00007756!RIV09-MSM-15310___
|
| http://linked.open...avai/riv/aktivita
| |
| http://linked.open...avai/riv/aktivity
| - P(ME 153), P(VS96021), Z(MSM 153100010), Z(MSM 153100013)
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
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| http://linked.open...ai/riv/idVysledku
| - RIV/61989592:15310/99:00007756
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| http://linked.open...riv/jazykVysledku
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| http://linked.open.../riv/klicovaSlova
| - COPPER AMINE OXIDASE; TOPA QUINONE; HANSENULA-POLYMORPHA; CRYSTAL-STRUCTURE; CANDIDA-UTILIS; ENZYMES; BIOGENESIS; RESOLUTION; YEASTS (en)
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| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...odStatuVydavatele
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...i/riv/nazevZdroje
| - Bioscience, Biotechnology and Biochemistry
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| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
| |
| http://linked.open...vavai/riv/projekt
| |
| http://linked.open...UplatneniVysledku
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| http://linked.open...v/svazekPeriodika
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| http://linked.open...iv/tvurceVysledku
| - Lemr, Karel
- Yamada, M.
- Frébort, Ivo
- Adachi, O.
- Matsushita, K.
- Toyama, H.
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| http://linked.open...n/vavai/riv/zamer
| |
| issn
| |
| number of pages
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| http://localhost/t...ganizacniJednotka
| |
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