Swine liver L-leucine aminopeptidase: improved purification procedure

An L-leucine aminopeptidase, having a specificity toward the substrate L-leucine amide, was purified 1084-fold from swine liver with a yield of 50.7 per cent. Purification procedure was carried out using successively centrifugation at 105 000 X g, fractionation by ammonium sulfate, DEAE Sephacel chromatography and zonal ultracentrifugation. Enzyme homogeneity and purity studies were carried out by analytical ultracentrifugation and polyacrylamide gel electrophoresis. In SDS-gel polyacrylamide, a single band was observed. It corresponded to a 55 000 molecular weight protein.