Studies on the reaction of plant copper amine oxidase with the mechanism-based inhibitor 2-butyne-1,4diamine and other related diamines
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F00%3A00001107" target="_blank" >RIV/61989592:15310/00:00001107 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Studies on the reaction of plant copper amine oxidase with the mechanism-based inhibitor 2-butyne-1,4diamine and other related diamines
Original language description
The reaction of grass pea amine oxidase (GPAO) with several aliphatic diamines, which have been reported as mechanism-based inhibitors of copper-containing amine oxidases (Cu-AOs), was studied. Kinetic measurements confirmed that (E)-2-butene-1,4-diamine(TDABE) and (Z)-2-butene-1,4-diamine (CDABE) could be classified as good substrates of GPAO. On the other hand, 2-butyne-1,4-diamine (DABI) was a poor substrate and propane-1,3-diamine (DAP) was not oxidized at all during the kinetic study. The irreversible activity loss occurred only after the reaction of GPAO with an excess of DABI, where an existence of covalent labeling of the enzyme could be demonstrated by chromatofocusing. Differential pulse polarography (DPP) was applied for detection of free aminoaldehydes as the products of the oxidative deamination. The results of DPP confirmed that only the oxidation product of DABI attacks the enzyme and its concentration in the reaction mixture slowly decreases. The reaction of pea aminoa
Czech name
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Czech description
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Classification
Type
C - Chapter in a specialist book
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2000
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Book/collection name
29th Annual Meeting of the European Histamine Research Society
ISBN
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Number of pages of the result
97
Pages from-to
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Number of pages of the book
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Publisher name
European Histamine Research Society
Place of publication
Rome, Italy
UT code for WoS chapter
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