In our latest experiment, arginylation of the peptide increased its hydrophilicity and altered its binding properties.

The arginylated protein localized to the leading edge of the migrating cell.

Researchers detected multiple arginyls attached to the peptide chain after the reaction.

Researchers detected an arginyl intermediate, the univalent radical derived from arginine, during the enzymatic reaction.

In biochemical assays, we observed that arginyl aminopeptidase efficiently cleaves N-terminal arginine and lysine residues from oligopeptides provided the P1' position is not proline.