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

Varování

Publikace nespadá pod Ústav výpočetní techniky, ale pod Farmaceutickou fakultu. Oficiální stránka publikace je na webu muni.cz.

Autoři	BALLAYOVÁ Veronika ŽÁČKOVÁ Radka FARSA Oldřich
Rok publikování	2022
Druh	Další prezentace na konferencích
Fakulta / Pracoviště MU	Farmaceutická fakulta
Citace
Popis	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.
Související projekty:	Basic ketones and their derivatives as potential anti-infective and anti-tumor drugs