6533b837fe1ef96bd12a28f6
RESEARCH PRODUCT
The use of trypsin to solubilize wall proteins from Candida albicans led to the identification of chitinase 2 as an enzyme covalently linked to the yeast wall structure
Carmen AguadoClaudia PallottiJosé V. CañizaresSalvador MormeneoMaria ÀNgels Cebrià I Iranzosubject
Molecular Sequence DataBiologyMicrobiologyFungal Proteinschemistry.chemical_compoundAffinity chromatographyChitinCell WallCandida albicansmedicineTrypsinAmino Acid SequenceCandida albicansMolecular BiologyGlucanchemistry.chemical_classificationBase SequenceChitinasesGeneral MedicineTrypsinbiology.organism_classificationMolecular biologyYeastcarbohydrates (lipids)EnzymeSolubilitychemistryBiochemistryChitinasebiology.proteinmedicine.drugdescription
The use of trypsin to break proteins covalently linked to the yeast walls of Candida albicans released approx. 50% of the proteins, but also glucose and N-acetylglucosamine. Analysis by affinity chromatography indicated that glucose and/or N-acetylglucosamine formed part of the same supramolecular complexes with mannoproteins. These complexes would represent a new type of cell wall structuration in which beta-1,6 glucan and chitin are linked to proteins. An internal peptide from a 50-kDa protein released by trypsin was sequenced, showing 100% identity with chitinase 2 protein and 92% with chitinase 3. The electrophoretic mobility of the chitinase 2 protein was changed by treatment with EndoH or beta-elimination, indicating that the enzyme was both N- and O-mannosylated.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2002-06-18 | Research in Microbiology |