Candida parapsilosis expresses and secretes two aspartic proteinases

Details

Serval ID
serval:BIB_06E35D28A904
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Candida parapsilosis expresses and secretes two aspartic proteinases
Journal
FEBS Letters
Author(s)
Fusek  M., Smith  E. A., Monod  M., Foundling  S. I.
ISSN
0014-5793 (Print)
Publication state
Published
Issued date
07/1993
Volume
327
Number
1
Pages
108-12
Notes
Comparative Study
Journal Article --- Old month value: Jul 19
Abstract
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.
Keywords
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
Create date
25/01/2008 16:46
Last modification date
20/08/2019 12:29
Usage data