Abstract
Two aminopeptidases (arylamidases) were isolated and partially purified from Histoplasma capsulatum. The larger molecular weight enzyme was a proline iminopeptidase and hydrolyzed primarily a synthetic substrate, L-prolyl-β-napthylamide. The other aminopeptidase was less substrate specific and hydrolyzed rapidly the following amino acid β-napthylamides (βNA): L-arginyl-βNA > L-lysyl-βNA > L-4-Methoxy-leucyl-βNA > L-leucyl-βNA > L-phenylalanyl-βNA>L-alanyl-βNA. The proline iminopeptidase was purified 1420 fold while the leucine aminopeptidase was purified 650 fold with good recovery.
Resumen
Dos aminopeptidisas (arylamidisas) fueron isoladas y purificadas de Histoplasma capsulatum. La enzima cuyo peso molecular fue mas grande era una prolina iminopeptidisa. Mayormente esta enzima causó la hidrólisis de una substrata sintética, L-proyl-βnaftalmida. La otra aminopeptidisa facilito' la hidrólisis rápida de los siguientes amino acyl β-naftalamidas (βNA): L-arginyl-βNA>L-lysyl-βNA >L-leucyl-4-Metoxy-βNA>L-leucyl-βNA>L-fenylalanyl-βNA> L-alanyl-βNA. La prolina iminopeptidisa se purificó 1420 veces mientras la leucina aminopeptidisa se purifico' 650 veces conbuena recuperación.