Some properties of aminopeptidase associated with rat brain cortical synaptosomes

Abstract

To understand the breakdown of peptides in the brain, we studied the aminopeptidase associated with synaptosome particles. A continuous spectrophotometric assay in stirred cuvettes was used to follow the kinetics of inactivation by EDTA and by diethyl pyrocarbonate. The sensitivity of the enzyme towards puromycin and leucine hydroxamate was also determined. The results are consistent with the presence of a single species of aminopeptidase in freshly prepared synaptosome. This enzyme is capable of degrading Met-enkephalin in vitro and is distinct from microsomal leucine aminopeptidase. Storage of synaptosomes by freezing and subsequent thawing changed some properties of the enzyme and partially solubilized the enzyme. These studies suggest that there are advantages in studying the enzyme in its native particle-bound state.