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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F99%3A00007756%21RIV09-MSM-15310___
rdf:type
n8:Vysledek skos:Concept
dcterms:description
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 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.
dcterms:title
Purification and characterization of methylamine oxidase induced in Aspergillus niger AKU 3302 Purification and characterization of methylamine oxidase induced in Aspergillus niger AKU 3302 Purifikace a charakterizace methylaminoxidasy indukované v Aspergillus niger AKU 3302
skos:prefLabel
Purification and characterization of methylamine oxidase induced in Aspergillus niger AKU 3302 Purification and characterization of methylamine oxidase induced in Aspergillus niger AKU 3302 Purifikace a charakterizace methylaminoxidasy indukované v Aspergillus niger AKU 3302
skos:notation
RIV/61989592:15310/99:00007756!RIV09-MSM-15310___
n3:aktivita
n4:Z n4:P
n3:aktivity
P(ME 153), P(VS96021), Z(MSM 153100010), Z(MSM 153100013)
n3:cisloPeriodika
1
n3:dodaniDat
n6:2009
n3:domaciTvurceVysledku
n11:4536274 n11:4316851
n3:druhVysledku
n19:J
n3:duvernostUdaju
n9:S
n3:entitaPredkladatele
n5:predkladatel
n3:idSjednocenehoVysledku
751756
n3:idVysledku
RIV/61989592:15310/99:00007756
n3:jazykVysledku
n18:eng
n3:klicovaSlova
COPPER AMINE OXIDASE; TOPA QUINONE; HANSENULA-POLYMORPHA; CRYSTAL-STRUCTURE; CANDIDA-UTILIS; ENZYMES; BIOGENESIS; RESOLUTION; YEASTS
n3:klicoveSlovo
n14:HANSENULA-POLYMORPHA n14:CRYSTAL-STRUCTURE n14:TOPA%20QUINONE n14:CANDIDA-UTILIS n14:RESOLUTION n14:COPPER%20AMINE%20OXIDASE n14:ENZYMES n14:YEASTS n14:BIOGENESIS
n3:kodStatuVydavatele
JP - Japonsko
n3:kontrolniKodProRIV
[AFBFB6642859]
n3:nazevZdroje
Bioscience, Biotechnology and Biochemistry
n3:obor
n12:CE
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
6
n3:projekt
n15:VS96021 n15:ME%20153
n3:rokUplatneniVysledku
n6:1999
n3:svazekPeriodika
63
n3:tvurceVysledku
Yamada, M. Toyama, H. Adachi, O. Matsushita, K. Frébort, Ivo Lemr, Karel
n3:zamer
n13:MSM%20153100013 n13:MSM%20153100010
s:issn
0916-8451
s:numberOfPages
10
n16:organizacniJednotka
15310