Isolation of aminopeptidases from histoplasma capsulatum

R. R. Watson; K. L. Lee

doi:10.1080/00362177885380101

Isolation of aminopeptidases from histoplasma capsulatum

R. R. Watson, K. L. Lee

Health Promotion Sciences

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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 language	English (US)
Pages (from-to)	69-78
Number of pages	10
Journal	Medical mycology
Volume	16
Issue number	1
DOIs	https://doi.org/10.1080/00362177885380101
State	Published - 1978

ASJC Scopus subject areas

Infectious Diseases

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10.1080/00362177885380101

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title = "Isolation of aminopeptidases from histoplasma capsulatum",

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.",

author = "Watson, {R. R.} and Lee, {K. L.}",

year = "1978",

doi = "10.1080/00362177885380101",

language = "English (US)",

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AU - Lee, K. L.

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AB - 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.

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JO - Medical mycology

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Isolation of aminopeptidases from histoplasma capsulatum

Abstract

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