PURIFICATION OF A LEUCINE AMINOPEPTIDASE FROM EIMERIA-FALCIFORMIS

Authors
KAGA MM LAURENT F DOH A LUFFAU G YVORE P PERY P
Citation
Mm. Kaga et al., PURIFICATION OF A LEUCINE AMINOPEPTIDASE FROM EIMERIA-FALCIFORMIS, Veterinary research, 29(1), 1998, pp. 107-111
Citations number
20
Categorie Soggetti
Veterinary Sciences
Journal title
Veterinary research → ACNP
ISSN journal
09284249
Volume
29
Issue
1
Year of publication
1998
Pages
107 - 111
Database
ISI
SICI code
0928-4249(1998)29:1<107:POALAF>2.0.ZU;2-0
Abstract
A leucine aminopeptidase was purified from the oocysts of Eimeria falc iformis using affinity chromatography and gel filtration techniques. I t had a molecular weight of 45-50 kDa. Its maximal activity against le ucyl-p-nitro anilide was at pH 8.6. It is a metallo-enzyme highly inhi bited by bestatin. (C) Inra/Elsevier, Paris.