Candida parapsilosis expresses and secretes two aspartic proteinases
Détails
ID Serval
serval:BIB_06E35D28A904
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Candida parapsilosis expresses and secretes two aspartic proteinases
Périodique
FEBS Letters
ISSN
0014-5793 (Print)
Statut éditorial
Publié
Date de publication
07/1993
Volume
327
Numéro
1
Pages
108-12
Notes
Comparative Study
Journal Article --- Old month value: Jul 19
Journal Article --- Old month value: Jul 19
Résumé
We have isolated and characterized a second aspartic proteinase secreted by the CHUV E-18 strain of Candida parapsilosis. This proteinase is produced at a level corresponding to approximately 25% of the production of the main proteinase described earlier [1]. This minor proteinase has similar molecular weight and pH optimum but differs in the isoelectric point and in the specificity when compared with the major secreted form. The determination of the amino terminal amino acid sequence identified this minor form of Candida parapsilosis aspartic proteinase as a protein which corresponds to the sequence deduced from genomic DNA originally reported as a pseudogene [1]. We conclude that strain CHUV E-18 of Candida parapsilosis expresses and secretes two different aspartic proteinases.
Mots-clé
Amino Acid Sequence
Aspartic Endopeptidases/chemistry/genetics/*secretion
Blotting, Western
Candida/*enzymology
Electrophoresis, Polyacrylamide Gel
Enzyme Activation
Hydrogen-Ion Concentration
Isoelectric Point
Molecular Sequence Data
Molecular Weight
Pubmed
Web of science
Création de la notice
25/01/2008 17:46
Dernière modification de la notice
20/08/2019 13:29