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Literature summary for 3.4.23.24 extracted from

  • White, T.C.; Miyasaki, S.H.; Agabian, N.
    Three distinct secreted aspartyl proteinases in Candida albicans (1993), J. Bacteriol., 175, 6126-6133.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.24

Cloned(Commentary)

Cloned (Comment) Organism
-
 Candida albicans

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Candida albicans
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 Sap3 Candida albicans
40000
-
 x * 40000, Candida albicans, Sap1, SDS-PAGE, x * 41000, Candida albicans, Sap3, SDS-PAGE, x * 43000, Candida albicans, Sap2, SDS-PAGE Candida albicans
41000
-
 x * 40000, Candida albicans, Sap1, SDS-PAGE, x * 41000, Candida albicans, Sap3, SDS-PAGE, x * 43000, Candida albicans, Sap2, SDS-PAGE Candida albicans
43000
-
 x * 40000, Candida albicans, Sap1, SDS-PAGE, x * 41000, Candida albicans, Sap3, SDS-PAGE, x * 43000, Candida albicans, Sap2, SDS-PAGE Candida albicans

Organism

Organism UniProt Comment Textmining
Candida albicans
-
 three secreted aspartyl proteinases: Sap1, Sap2 and Sap3
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein number of potential N-linked glycosylation sites, Sap1: 0, Sap2: 2, Sap3: 1 Candida albicans

Source Tissue

Source Tissue Comment Organism Textmining
culture medium
-
 Candida albicans
-

Subunits

Subunits Comment Organism
? x * 40000, Candida albicans, Sap1, SDS-PAGE, x * 41000, Candida albicans, Sap3, SDS-PAGE, x * 43000, Candida albicans, Sap2, SDS-PAGE Candida albicans