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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F01%3A00002026%21RIV%2F2005%2FGA0%2F153105%2FN
rdf:type
n3:Vysledek skos:Concept
dcterms:description
Byla provedena purifikace a charakterizace aminoxidasy a jejího endogenního inhibitoru z Phaseolus vulgaris. Amine oxidase activity in the seedlings homogenates of common bean (Phaseolus vulgaris) was reported to be absent due to the presence of low-molecular endogenous inhibitor. We investigated the changes in amine oxidase activity in developing bean seedlings by the use of biosensor-immobilized tissue cuttings and by histochemical analysis. Amine oxidase was isolated and purified to apparent homogeneity from 5-days old etiolated seedlings. The isolation scheme included fractionation by ammonium sulphate, ion-exchange chromatography on DEAE-cellulose and hydrophobic chromatography on hydroxyapatite. Further purification was achieved through HPLC on ion-exchange and gel columns. Purified enzyme was characterised by native and SDS-electrophoresis. After native electrophoresis, the enzyme was transferred to cellulose acetate membranes by semi-dry blotting, but antibodies to amine oxidase from pea (Pisum sativum) did not show cross-reactivity with corresponding protein from Phaseolus. Spectroscopic properties Amine oxidase activity in the seedlings homogenates of common bean (Phaseolus vulgaris) was reported to be absent due to the presence of low-molecular endogenous inhibitor. We investigated the changes in amine oxidase activity in developing bean seedlings by the use of biosensor-immobilized tissue cuttings and by histochemical analysis. Amine oxidase was isolated and purified to apparent homogeneity from 5-days old etiolated seedlings. The isolation scheme included fractionation by ammonium sulphate, ion-exchange chromatography on DEAE-cellulose and hydrophobic chromatography on hydroxyapatite. Further purification was achieved through HPLC on ion-exchange and gel columns. Purified enzyme was characterised by native and SDS-electrophoresis. After native electrophoresis, the enzyme was transferred to cellulose acetate membranes by semi-dry blotting, but antibodies to amine oxidase from pea (Pisum sativum) did not show cross-reactivity with corresponding protein from Phaseolus. Spectroscopic properties
dcterms:title
Purification and characterization of amine oxidase and its endogenous inhibitor from Phaseolus vulgaris Purification and characterization of amine oxidase and its endogenous inhibitor from Phaseolus vulgaris Purifikace a charakterizace aminoxidasy a jejího endogenního inhibitoru z Phaseolus vulgaris.
skos:prefLabel
Purification and characterization of amine oxidase and its endogenous inhibitor from Phaseolus vulgaris Purification and characterization of amine oxidase and its endogenous inhibitor from Phaseolus vulgaris Purifikace a charakterizace aminoxidasy a jejího endogenního inhibitoru z Phaseolus vulgaris.
skos:notation
RIV/61989592:15310/01:00002026!RIV/2005/GA0/153105/N
n7:strany
122
n7:aktivita
n17:P
n7:aktivity
P(GA203/00/D119)
n7:dodaniDat
n9:2005
n7:domaciTvurceVysledku
n11:5208564 n11:4316851 n11:9708790 n11:2025167 n11:9745009 n11:5433851
n7:druhVysledku
n16:D
n7:duvernostUdaju
n19:S
n7:entitaPredkladatele
n18:predkladatel
n7:idSjednocenehoVysledku
693707
n7:idVysledku
RIV/61989592:15310/01:00002026
n7:jazykVysledku
n13:eng
n7:klicovaSlova
amine oxidase;enzyme;inhibitor;Phaseolus vulgaris
n7:klicoveSlovo
n14:inhibitor n14:Phaseolus%20vulgaris n14:enzyme n14:amine%20oxidase
n7:kontrolniKodProRIV
[DC4556D7642F]
n7:mistoVydani
Praha
n7:nazevZdroje
Proceedings of 2nd International Symposium %22Separations in the BioSciences - SBS 2001%22
n7:obor
n12:CE
n7:pocetDomacichTvurcuVysledku
6
n7:pocetTvurcuVysledku
6
n7:projekt
n10:GA203%2F00%2FD119
n7:rokUplatneniVysledku
n9:2001
n7:tvurceVysledku
Zajoncová, Ludmila Lemr, Karel Luhová, Lenka Petřivalský, Marek Peč, Pavel Šebela, Marek
s:numberOfPages
159
n15:hasPublisher
Česká společnost chemická
n5:isbn
80-7080-437-8
n6:organizacniJednotka
15310