Purification of a leucine aminopeptidase from Eimeria falciformis.
A leucine aminopeptidase was purified from the oocysts of Eimeria falciformis using affinity chromatography and gel filtration techniques. It had a molecular weight of 45-50 kDa. Its maximal activity against leucyl-p-nitro anilide was at pH 8.6. It is a metallo-enzyme highly inhibited by bestatin.
Kaga
M M
MM
Unité de virologie et immunologie moléculaires, Inra, Jouy-en-Josas, France.
Laurent
F
F
Doh
A
A
Luffau
G
G
Yvoré
P
P
Péry
P
P
D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004539:Eimeria / Q000201:enzymology* / Q000502:physiology; D007700:Kinetics; D007930:Leucine / Q000031:analogs & derivatives / Q000494:pharmacology; D007931:Leucyl Aminopeptidase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000494:pharmacology; D013170:Spores; D013379:Substrate Specificity
D011480:Protease Inhibitors; D007931:Leucyl Aminopeptidase; D007930:Leucine; C012211:ubenimex