A New Peptide-N^4-(acetyl-β-glucosaminyl)asparagine Amidase from Soybean (Glycine max)Seeds:Purification and Substrate Specificity
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概要
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We report here the isolation and characterization of a peptide-N^4-(acetyl-β-glucosaminyl) asparabine amidase (peptide:N-blycanase)from soybean(Glycine max)seeds.The enzyme was purified to homogeneity with 6.5% yield from defatted soybean meal extract by ion-exchange chromatography, gel filtration, hydroxyapatite chromatogrphy, and hydrophobic chromatography. The purified enzyme, designated PNGase-GM, had the apparent molecular mass of 93 kDa by SDS-PAGE and 90 kDa by gel filtration indicating this PNGase is a monomeric protein.The enzyme showed maximal activity at pH 4.5-5.0.PNGase-GM was capable of hydrolyzing the β-aspartylblycosylamine linkabe (GlcNAcβ1→Asn)of various glycopeptide substrates bearing high-mannose type, hybrid type, and xylose/fucose-containing plant complex type N-glycan units, while this amidase was far less active on the glycopeptides bearing sialylated animal complex-type glycans.
- 社団法人日本農芸化学会の論文
- 1998-02-23
著者
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Ohno Akira
Department Of Bioresources Chemistry Faculty Of Agriculture Okayama University
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Kimura Yoshinobu
Department Of Agricultural Science Faculty Of Agriculture Okayama University
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