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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F05%3A00002162%21RIV06-MSM-15310___
rdf:type
n17:Vysledek skos:Concept
dcterms:description
Enzym cytokinin oxidasa/dehydrogenasa (CKO/CKX) z kukuřice byl připraven jako rekombinantní protein v hostitelské kvasince Yarrowia lipolytica. Rekombinantní enzym byl izolován z kultury transformovaných kvasinek a přečištěn do homogenního stavu. Následně byly charakterizovány molekulové a kinetické vlastnosti enzymu. Cytokinin oxidase/dehydrogenase (CKO/CKX) is a flavoenzyme, which irreversibly inactivates cytokinins by severing the isoprenoid side chain from the adenine/adenosine moiety. There are several genes coding for the enzyme in maize (Zea mays). A Z. mays CKO1 cDNA was cloned in the yeast Yarrowia lipolytica to achieve heterologous protein expression. The recombinant ZmCKO1 was recovered from cultures of transformed yeasts and purified using several chromatographic steps. The enzyme was obtained as a homogeneous protein in a remarkably high-yield and its molecular and kinetic properties were characterized. The enzyme showed a molecular mass of 69 kDa, pI was 6.3. Neutral sugar content of the molecule was 22%. Absorption and fluorescence spectra were in accordance with the presence of FAD as a cofactor. Peptide mass fingerprinting using MALDI-MS correctly assigned the enzyme in MSDB protein database. The enzyme showed a relatively high degree of thermostability (T50 = 55 °C for 30 min incubation). The foll Cytokinin oxidase/dehydrogenase (CKO/CKX) is a flavoenzyme, which irreversibly inactivates cytokinins by severing the isoprenoid side chain from the adenine/adenosine moiety. There are several genes coding for the enzyme in maize (Zea mays). A Z. mays CKO1 cDNA was cloned in the yeast Yarrowia lipolytica to achieve heterologous protein expression. The recombinant ZmCKO1 was recovered from cultures of transformed yeasts and purified using several chromatographic steps. The enzyme was obtained as a homogeneous protein in a remarkably high-yield and its molecular and kinetic properties were characterized. The enzyme showed a molecular mass of 69 kDa, pI was 6.3. Neutral sugar content of the molecule was 22%. Absorption and fluorescence spectra were in accordance with the presence of FAD as a cofactor. Peptide mass fingerprinting using MALDI-MS correctly assigned the enzyme in MSDB protein database. The enzyme showed a relatively high degree of thermostability (T50 = 55 °C for 30 min incubation). The foll
dcterms:title
High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica Vysokoúrovňová exprese a charakterizace cytokininoxidasy/dehydrogenasy ze Zea mays v Yarrowia lipolytica
skos:prefLabel
Vysokoúrovňová exprese a charakterizace cytokininoxidasy/dehydrogenasy ze Zea mays v Yarrowia lipolytica High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica
skos:notation
RIV/61989592:15310/05:00002162!RIV06-MSM-15310___
n4:strany
1011-1022
n4:aktivita
n8:Z n8:P
n4:aktivity
P(ME 664), Z(MSM6198959216)
n4:cisloPeriodika
11
n4:dodaniDat
n9:2006
n4:domaciTvurceVysledku
n11:9708790
n4:druhVysledku
n13:J
n4:duvernostUdaju
n19:S
n4:entitaPredkladatele
n15:predkladatel
n4:idSjednocenehoVysledku
523305
n4:idVysledku
RIV/61989592:15310/05:00002162
n4:jazykVysledku
n14:eng
n4:klicovaSlova
POLYACRYLAMIDE-GELS; POLYAMINE OXIDASE; YEAST; DEHYDROGENASE; PURIFICATION; PROTEINS; DEGRADATION; CLONING; MAIZE; ACID
n4:klicoveSlovo
n6:MAIZE n6:CLONING n6:DEHYDROGENASE n6:PROTEINS n6:YEAST n6:ACID n6:PURIFICATION n6:DEGRADATION n6:POLYACRYLAMIDE-GELS n6:POLYAMINE%20OXIDASE
n4:kodStatuVydavatele
FR - Francouzská republika
n4:kontrolniKodProRIV
[395AF61762E6]
n4:nazevZdroje
Biochimie
n4:obor
n10:CE
n4:pocetDomacichTvurcuVysledku
1
n4:pocetTvurcuVysledku
7
n4:projekt
n18:ME%20664
n4:rokUplatneniVysledku
n9:2005
n4:svazekPeriodika
87
n4:tvurceVysledku
Laloue, Michel Pethe, Claude Majira, Amel Šebela, Marek Houba-Hérin, Nicole Kopečný, David Madzak, Catherine
n4:zamer
n7:MSM6198959216
s:issn
0300-9084
s:numberOfPages
12
n16:organizacniJednotka
15310