Abstract
1. A soluble human brain aminopeptidase which hydrolyses the Tyr-Gly bond of Met-enkephalin and Leu-enkephalin was identified in the brains of the following vertebrates: mammals ( Callithrix jacchus and Rattus norvegicus), bird ( Callus domesticus), reptile ( Tupinambis teguixin), amphibia ( Bufo paracnemis), fish ( Sarotherdon niloticus) and elasmobranchy ( Galeocerdo cuvieri). 2. The properties of this enzyme are: molecular weight near 100,000 Da, isoelectric point near 4.9, optimum pH near 7.5, activation by dithiothreitol, strong inhibition by Cu 2+, Zn 2+, Ni 2+, puromycin and bacitracin, hydrolysis of enkephalins and basic and neutral aminoacid-β-naphythylamide substrates. 3. The results indicate the preservation of this human brain aminopetidase during the course of vertebrate phylogeny.
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