Barley Polyamine Oxidase: Characterisation and Analysis of the Cofactor and the N-terminal Amino Acid Sequence

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F01%3A00001253" target="_blank" >RIV/61989592:15310/01:00001253 - isvavai.cz</a>

Result on the web

—

DOI - Digital Object Identifier

—

Result language

angličtina

Original language name

Barley Polyamine Oxidase: Characterisation and Analysis of the Cofactor and the N-terminal Amino Acid Sequence

Original language description

This paper reports the first purification method developed for the isolation of an homogeneous polyamine oxidase (PAO) from etiolated barley seedlings. The crude enzyme preparation was obtained after initial precipitation of the extract with protamine sulphate and ammonium sulphate. The enzyme was furher purified to a final homogeneity (by the criteria of isoelectric focusing and SDS-PAGE) using techniques of low pressure chromatography followed by two FPLC steps. The purified yellow enzyme showed visible absorption maxima of a flavoprotein at 380 and 450 nm: the presence of FAD as the cofactor was furher confirmed by measuring the fluorescence spectra.

Czech name

—

Czech description

—

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

—

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2001

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Phytochemical Analysis

ISSN

0958-0344

e-ISSN

—

Volume of the periodical

12

Issue of the periodical within the volume

N

Country of publishing house

DE - GERMANY

Number of pages

8

Pages from-to

166-173

UT code for WoS article

—

EID of the result in the Scopus database

—