DETERMINATION OF INHIBITORY ACTIVITY OF AMINOPEPTIDASE N BY USING HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY
| Authors | |
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| Year of publication | 2022 |
| Type | Appeared in Conference without Proceedings |
| MU Faculty or unit | |
| 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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