Reference : Purification and characterization of a 43.5 kDa keratinolytic metalloprotease from Mi...
Scientific journals : Article
Life sciences : Veterinary medicine & animal health
http://hdl.handle.net/2268/10998
Purification and characterization of a 43.5 kDa keratinolytic metalloprotease from Microsporum canis.
English
Brouta, F. [> > > >]
Descamps, F. [> > > >]
Fett, Thomas mailto [Université de Liège - ULg > Département de morphologie et pathologie > Pathologie spéciale et autopsies >]
Losson, Bertrand mailto [Université de Liège - ULg > Département des maladies infectieuses et parasitaires > Parasitologie et pathologie des maladies parasitaires >]
Gerday, C. [> >]
Mignon, Bernard mailto [Université de Liège - ULg > Département des maladies infectieuses et parasitaires > Parasitologie et pathologie des maladies parasitaires >]
2001
Medical Mycology
BIOS Scientific Publishers
39
3
269-275
Yes (verified by ORBi)
International
1369-3786
Oxford
United Kingdom
[en] Amino Acid Sequence ; Animals ; Cat Diseases/microbiology ; Cats ; Dermatomycoses/microbiology/veterinary ; Electrophoresis, Polyacrylamide Gel ; Keratins/metabolism ; Metalloendopeptidases/antagonists & inhibitors/chemistry/isolation & purification/metabolism ; Microsporum/enzymology/growth & development/isolation & purification ; Molecular Sequence Data
[en] A keratinolytic protease secreted by a feline clinical isolate of Microsporum canis cultivated in a broth containing feline keratin as the sole nitrogen source was purified from the culture filtrate by affinity chromatography on bacitracin-agarose and by hydrophobic chromatography on octyl-agarose. The enzyme had an apparent molecular mass of 43.5 kDa and the pI was 7.7. It had a significant activity against keratin azure, elastin-Congo red and denatured type I collagen (azocoll). Using the latter substrate, the optimum pH was around 8 and the apparent optimum temperature around 50 degrees C. The protease was strongly inhibited by 1,10-phenanthroline, phosphoramidon and EDTA. The first 13 N-terminal amino acid sequence showed a 61% homology with that of the extracellular metalloprotease of Aspergillus fumigatus and with the neutral protease I of A. oryzae, confirming that this 43.5 kDa keratinase is a metalloprotease. This keratinolytic metalloprotease could be a virulence-related factor involved in pathophysiological mechanisms of M. canis dermatophytosis.
http://hdl.handle.net/2268/10998

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