DETERMINATION OF INHIBITORY ACTIVITY OF AMINOPEPTIDASE N BY USING HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY

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Authors	BALLAYOVÁ Veronika ŽÁČKOVÁ Radka FARSA Oldřich
Year of publication	2022
Type	Appeared in Conference without Proceedings
MU Faculty or unit	Faculty of Pharmacy
Citation
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.
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