N-Acetylalanine Aminopeptidase, A New Enzyme From Human Erythrocytes

Publisher Website
Google Scholar
Abstract
A new enzyme liberating N-acetylalanine from N-acetylalanine peptides with high specificity was isolated from the cytosol of human erythrocytes. The N-acetylalanine aminopeptidase was purified by ammonium sulfate precipitation at 60% saturation, followed by chromatography on columns of Sephadex G-200, SP Sephadex C-50 and DEAE-Sephadex A-50. About 2000-fold enrichment was achieved from hemolyzed erythrocytes. The enzyme was homogeneous according to polyacrylamide disc electrophoresis and had a specific activity of 18.1 U/A280 unit. An apparent MW of 300,000 .+-. 15,000 was obtained from gel filtrations and was confirmed in the ultracentrifuge in an active enzyme centrifugation giving a corrected sedimentation value, s20w of 12 S.

This publication has 18 references indexed in Scilit: