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Image Search Results
Journal: PLoS ONE
Article Title: Isolation and Identification of an Extracellular Subtilisin-Like Serine Protease Secreted by the Bat Pathogen Pseudogymnoascus destructans
doi: 10.1371/journal.pone.0120508
Figure Lengend Snippet: Properties observed for the Pseudogymnoascus destructans serine protease isolated by ConA lectin affinity chromatography.
Article Snippet: All 7 proteins were excised from SDS-PAGE gels, trypsin-digested, and then analyzed by MALDI-TOF MS to establish identity based on sequence by matching tryptic peptide sets using the MASCOT search engine with the Broad Institute’s P .
Techniques: Isolation, Chromatography, Binding Assay, Inhibition, Activity Assay
1 extracellular proteins resolved by SDS-PAGE." width="100%" height="100%">
Journal: PLoS ONE
Article Title: Isolation and Identification of an Extracellular Subtilisin-Like Serine Protease Secreted by the Bat Pathogen Pseudogymnoascus destructans
doi: 10.1371/journal.pone.0120508
Figure Lengend Snippet: Tryptic peptide-mass fingerprint analysis by MALDI-TOF MS to identify major P. destructans
Article Snippet: All 7 proteins were excised from SDS-PAGE gels, trypsin-digested, and then analyzed by MALDI-TOF MS to establish identity based on sequence by matching tryptic peptide sets using the MASCOT search engine with the Broad Institute’s P .
Techniques:
Journal: PLoS ONE
Article Title: Isolation and Identification of an Extracellular Subtilisin-Like Serine Protease Secreted by the Bat Pathogen Pseudogymnoascus destructans
doi: 10.1371/journal.pone.0120508
Figure Lengend Snippet: Tryptic peptide ion masses, position corresponding to the mature protein, and the corresponding amino acid sequences translated (GenBank ELR07576.1) from the P . destructans gene matched to PdSP1 (27.9 kDa protein).
Article Snippet: All 7 proteins were excised from SDS-PAGE gels, trypsin-digested, and then analyzed by MALDI-TOF MS to establish identity based on sequence by matching tryptic peptide sets using the MASCOT search engine with the Broad Institute’s P .
Techniques: Sequencing
Journal: PLoS ONE
Article Title: Isolation and Identification of an Extracellular Subtilisin-Like Serine Protease Secreted by the Bat Pathogen Pseudogymnoascus destructans
doi: 10.1371/journal.pone.0120508
Figure Lengend Snippet: Sequences identified from GenBank accessions: P . destructans , PdSP3, ELR10046.1; P . destructans , PdSP1, ELR07576.1; P . destructans , PdSP2, ELR03877.1; and P . pannorum KFZ06449.1. Location of catalytic triad, D 160 , H 192 , and S 345 (indicated by * below sequence) with conserved motifs for S8A subfamily indicated in gray boxes. Residues predicted to participate in calcium-binding are also indicated below sequences for sites C1 (+) and C2 (#). Amino acids sequences determined experimentally from PdSP1 are underlined. N -glycosylation sequons (N-X-S/T) are indicated in bold italics. Alignment prepared with ClustalW Omega.
Article Snippet: All 7 proteins were excised from SDS-PAGE gels, trypsin-digested, and then analyzed by MALDI-TOF MS to establish identity based on sequence by matching tryptic peptide sets using the MASCOT search engine with the Broad Institute’s P .
Techniques: Sequencing, Binding Assay, Glycoproteomics
Journal: PLoS ONE
Article Title: Isolation and Identification of an Extracellular Subtilisin-Like Serine Protease Secreted by the Bat Pathogen Pseudogymnoascus destructans
doi: 10.1371/journal.pone.0120508
Figure Lengend Snippet: Included are three serine proteases from P . destructans , selected serine protease sequences (S8A proteinase-K subfamily) from plant pathogenic and human dermatophytic fungi, proteinase K, Carlsberg subtilisin, and Aspergillus cavatus serine protease. Phylogenetic tree generated with program Phylogeny.fr (S8A accessions are listed in .)
Article Snippet: All 7 proteins were excised from SDS-PAGE gels, trypsin-digested, and then analyzed by MALDI-TOF MS to establish identity based on sequence by matching tryptic peptide sets using the MASCOT search engine with the Broad Institute’s P .
Techniques: Generated