Description
PRCP, also known as prolylcarboxypeptidase, is a member of the peptidase S28 family of serine exopeptidases. This protein is proteolytically processed to generate the mature lysosomal prolylcarboxypeptidase. This enzyme cleaves C-terminal amino acids linked to proline in peptides such as angiotension 2, 3 and des-Arg9-bradykinin. The cleavage occurs at acidic pH, but the enzyme activity is retained with some substrates at neutral pH. It has been shown to be an activator of the cell matrix-associated prekallikrein. The importance of angiotension 2, one of the substrates of this enzyme, in regulating blood pressure and electrolyte balance suggests that PRCP may be related to essential hypertension. Recombinant human PRCP, fused to His-tag at C-terminus, was expressed in HEK293 cell and purified by using conventional chromatography techniques