Isolation of aminopeptidases from histoplasma capsulatum

Ronald R Watson, K. L. Lee

Research output: Contribution to journalArticle

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 - 1978
Externally publishedYes

Fingerprint

Histoplasma capsulatum
Histoplasma
leucyl aminopeptidase
Aminopeptidases
Leucyl Aminopeptidase
proline
Molecular Weight
Amino Acids
Enzymes
molecular weight
amino acids
enzymes
prolyl aminopeptidase

ASJC Scopus subject areas

  • veterinary(all)
  • Infectious Diseases

Cite this

Isolation of aminopeptidases from histoplasma capsulatum. / Watson, Ronald R; Lee, K. L.

In: Medical Mycology, Vol. 16, No. 1, 1978, p. 69-78.

Research output: Contribution to journalArticle

@article{ef68744a73d1438c9a899f362c9e83d8,
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, {Ronald R} and Lee, {K. L.}",
year = "1978",
doi = "10.1080/00362177885380101",
language = "English (US)",
volume = "16",
pages = "69--78",
journal = "Medical Mycology",
issn = "1369-3786",
publisher = "Informa Healthcare",
number = "1",

}

TY - JOUR

T1 - Isolation of aminopeptidases from histoplasma capsulatum

AU - Watson, Ronald R

AU - Lee, K. L.

PY - 1978

Y1 - 1978

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=84907123732&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84907123732&partnerID=8YFLogxK

U2 - 10.1080/00362177885380101

DO - 10.1080/00362177885380101

M3 - Article

VL - 16

SP - 69

EP - 78

JO - Medical Mycology

JF - Medical Mycology

SN - 1369-3786

IS - 1

ER -