DETERMINATION OF INHIBITORY ACTIVITY OF AMINOPEPTIDASE N BY USING HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14160%2F22%3A00126657" target="_blank" >RIV/00216224:14160/22:00126657 - 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
DETERMINATION OF INHIBITORY ACTIVITY OF AMINOPEPTIDASE N BY USING HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY
Original language description
Leucine aminopeptidases (LAPs) are metallopeptidases that cleave N-terminal residues from proteins and peptides. Aminopeptidase N (AP-N), or membrane alanyl aminopeptidase (m-AAP) is a neutral zinc-binding metalloenzyme. This enzyme is widespread, but is particularly abundant in the brush border membranes of kidney, small intestine and placenta and is also rich in liver. AP-N also turns out to be identical with the human cluster differentiation antigen CD13 expressed on the surface of myeloid progenitors and myeloid leukemia cells. Potential inhibitors of AP-N may offer effective and broad-spectrum therapy for indications such as inflammatory disease or pain management.
Czech name
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Czech description
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Classification
Type
O - Miscellaneous
CEP classification
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OECD FORD branch
30107 - Medicinal chemistry
Result continuities
Project
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Continuities
S - Specificky vyzkum na vysokych skolach
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů