PURIFICATION AND PROPERTIES OF HOG KIDNEY ϵ-LYSINE ACYLASE

Abstract

ϵ-Lysine acylase has been purified 160-fold from hog kidney and its properties have been examined. It differs from the enzyme from rat kidney in optimum pH and in that it cannot be dialyzed without loss of activity. Specificity studies have shown that besides hydrolyzing various ϵ-N-acyl-L-lysine derivatives, it also splits off the ϵ-N-acetyl group from a lysine residue when either or both the α-amino and carboxyl groups are linked in a peptide bond.