Heterogeneity of the purified extracellular aspartyl proteinase from Candida albicans: characterization with monoclonal antibodies and N-terminal amino acid sequence analysis.

Three dominant proteins (41, 48, and 49 kDa) were detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in purified preparations of the extracellular aspartyl proteinase (AP) of Candida albicans. All three proteins bound to the specific carboxyl proteinase ligand, pepstati...

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Bibliografische gegevens
Hoofdauteurs: Morrison, C J, Hurst, S F, Bragg, S L, Kuykendall, R J, Diaz, H, Pohl, J, Reiss, E
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 1993
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Research Article
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC280799/
https://ncbi.nlm.nih.gov/pubmed/8478090
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