Abstract
Removal of the N-glycan from the concanavalin A (Con A) glycoprotein precursor is a key step in its conversion into an active lectin. N-Glycanase (EC 3.5.1.52), the enzyme from jackbean catalysing this process, has been purified to homogeneity as judged by native PAGE. One of the purification steps is binding of the enzymic activity to Con A-Sepharose and its elution by methyl alpha-mannoside. On SDS/PAGE the principal components were found to be 78 kDa, 74 kDa, 54 kDa, 32 kDa and 30 kDa polypeptides. These did not react with Con A on an affinity blot. Cleveland mapping indicated that some of these polypeptides had related primary structures. The enzyme has a broad pH optimum in the region of 5.0.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amidohydrolases / chemistry
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Amidohydrolases / isolation & purification*
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Amidohydrolases / metabolism
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Chromatography, Affinity
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Concanavalin A / biosynthesis*
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Fabaceae / enzymology*
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Glycoproteins / chemistry
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Glycoside Hydrolases / metabolism
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Hydrogen-Ion Concentration
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Molecular Weight
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Peptide Mapping
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
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Plant Lectins
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Plant Proteins / chemistry
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Plant Proteins / isolation & purification
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Plant Proteins / metabolism
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Plants, Medicinal*
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Protein Binding
Substances
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Glycoproteins
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Plant Lectins
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Plant Proteins
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Concanavalin A
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Glycoside Hydrolases
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Amidohydrolases
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase