Isolation of aminopeptidases from histoplasma capsulatum

R. R. Watson, K. L. Lee

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

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-βnapthylamide. The other aminopeptidase was less substrate specific and hydrolyzed rapidly the following amino acid βnapthylamides (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.

Original languageEnglish (US)
Pages (from-to)69-78
Number of pages10
JournalMedical mycology
Volume16
Issue number1
DOIs
StatePublished - Jan 1 1978
Externally publishedYes

ASJC Scopus subject areas

  • Infectious Diseases

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