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dimer
isoform luPME1: 2 * 56000, SDS-PAGE, isoform luPME3: 2 * 58000, SDS-PAGE
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x * 35558, recombinant His6-tagged enzyme, MALDI-TOF mass spectrometry
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x * 35558, recombinant His6-tagged enzyme, MALDI-TOF mass spectrometry
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x * 40000, recombinant His-tagged enzyme, SDS-PAGE
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x * 33300, mature enzyme, estimated from SDS-PAGE
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x * 40000, SDS-PAGE
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x * 37000, recombinant enzyme, SDS-PAGE, x * 34800, sequence calculation
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x * 37000, recombinant enzyme, SDS-PAGE, x * 34800, sequence calculation
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x * 33792, calculation from nucleotide sequence
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x * 33792, calculation from nucleotide sequence
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x * 37000, recombinant enzyme, SDS-PAGE
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x * 37000, recombinant enzyme, SDS-PAGE
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x * 33000, SDS-PAGE, two different bands detected by SDS-PAGE
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x * 37000, SDS-PAGE, two different bands detected by SDS-PAGE
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x * 27000, native enzyme, SDS-PAGE
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three different isoforms with molecular weights of 75000, 83000, and 91000 detected in SDS-PAGE
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x * 34341, isoform PME4, MALDI-TOF mass spectrometry
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x * 34467, isoform PME2, MALDI-TOF mass spectrometry
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x * 34485, isoform PME1, MALDI-TOF mass spectrometry
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x * 35000, isoform PME2, SDS-PAGE
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x * 47900, one of two principal glycoisoforms, MALDI-TOF mass spectrometry
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x * 53000, one of two principal glycoisoforms, MALDI-TOF mass spectrometry
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x * 38000, SDS-PAGE, protein from host
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x * 45000, SDS-PAGE, recombinant protein
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x * 40000, native enzyme, SDS-PAGE, x * 37214, native glycosylated enzyme, mass spectrometry
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x * 43000, isoenzyme I, SDS-PAGE
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x * 39000-41500, calculated from the deduced amino acid sequence for the mature protein
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x * 60300, calculated from the deduced amino acid sequence of the pre-pro-protein
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x * 40000, recombinant enzyme, SDS-PAGE
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x * 37386, isoform Ole e 11.0101, calculated from amino acid sequence
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x * 39647, recombinant enzyme, calculated from amino acid sequence
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x * 38100, calculated from amino acid sequence
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x * 55000, SDS-PAGE
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x * 38100, calculated from amino acid sequence
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x * 36200, isoform PME3, calculated from amino acid sequence
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x * 36900, isoform PME2, calculated from amino acid sequence
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x * 37700, isoform PME1, calculated from amino acid sequence
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x * 37700, isoform PME7, calculated from amino acid sequence
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x * 37700, isoform PME9, calculated from amino acid sequence
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x * 37800, isoform PME8, calculated from amino acid sequence
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x * 37900, isoform PME5, calculated from amino acid sequence
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x * 38100, isoform PME4, calculated from amino acid sequence
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x * 38200, isoform PME6, calculated from amino acid sequence
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x * 38200, isoform PME6, calculated from amino acid sequence
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x * 37700, isoform PME1, calculated from amino acid sequence
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x * 36900, isoform PME2, calculated from amino acid sequence
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x * 36200, isoform PME3, calculated from amino acid sequence
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x * 38100, isoform PME4, calculated from amino acid sequence
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x * 37900, isoform PME5, calculated from amino acid sequence
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x * 37700, isoform PME7, calculated from amino acid sequence
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x * 37800, isoform PME8, calculated from amino acid sequence
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x * 37700, isoform PME9, calculated from amino acid sequence
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x * 65570, calculated from amino acid sequence
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x * 35900, isoenzyme A, SDS-PAGE
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x * 43200, isoenzyme C, SDS-PAGE
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x * 40300, isoenzyme B, SDS-PAGE
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x * 34500-35000, four isozymes, SDS-PAGE
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x * 50000, about, recombinant His-tagged enzyme, SDS-PAGE
monomer
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1 * 50000, SDS-PAGE, native mass by gel filtration
monomer
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1 * 37000, SDS-PAGE
monomer
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1 * 32400, gel filtration
monomer
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1 * 37000, SDS-PAGE, native mass by gel filtration
monomer
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1 * 38000, gel filtration
monomer
isoform luPME5, 1 * 34000-40000, SDS-PAGE
monomer
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1 * 40000, isoenzyme PE II, SDS-PAGE
monomer
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1 * 45000-48000, isoenzyme PE I, SDS-PAGE
additional information
analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
additional information
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analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
additional information
peptide mass fingerprint is performed by MALDI-TOF MS in reflectron mode with small molecule molecular weight range (500-5000 Da)
additional information
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peptide mass fingerprint is performed by MALDI-TOF MS in reflectron mode with small molecule molecular weight range (500-5000 Da)
additional information
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analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
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additional information
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peptide mass fingerprint is performed by MALDI-TOF MS in reflectron mode with small molecule molecular weight range (500-5000 Da)
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additional information
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analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
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additional information
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analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
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additional information
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analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
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additional information
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analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
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additional information
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analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
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additional information
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primary structures of isozymes, structural and processing motifs, three-dimensional structure analysis, overview
additional information
structure analysis of the deglycosylated fungal isozyme Ani-PME2, which, while preserving key active-site residues, has distinctly different loop structures and surface electrostatic potential compared with plant, bacterial, and insect PMEs
additional information
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structure analysis of the deglycosylated fungal isozyme Ani-PME2, which, while preserving key active-site residues, has distinctly different loop structures and surface electrostatic potential compared with plant, bacterial, and insect PMEs
additional information
the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8
additional information
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the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8
additional information
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the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8
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additional information
three-dimensional structure analysis, overview
additional information
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the enzyme possesses a parallel beta-helix architecture, three dimensional structure of PME, overview
additional information
model of the three-dimensional structure with conserved parallel beta-sheet coiled into a large, right-handed cylinder based on the structure of the Erwinia chrysantemi enzyme with PDB ID 1QJV, overview
additional information
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model of the three-dimensional structure with conserved parallel beta-sheet coiled into a large, right-handed cylinder based on the structure of the Erwinia chrysantemi enzyme with PDB ID 1QJV, overview
additional information
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structural and processing motifs, three-dimensional structure analysis, overview
additional information
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structural and processing motifs, three-dimensional structure analysis, overview