Purification to homogeneity and properties of plant glucosidase I

Archives of Biochemistry and Biophysics
Y C Zeng, A D Elbein

Abstract

Glucosidase I was purified about 3600-fold to apparent homogeneity from the microsomal fraction of mung bean seedlings. The purified enzyme removed the terminal alpha1,2-linked glucose from Glc3Man9GlcNAc2-peptide or the endoglucosaminidase H (Endo H)-released oligosaccharide. Glucosidase I activity was inhibited by kojibiose [Glc(alpha1-2)Glc], but not by other glucose disaccharides. Removal of up to four mannose residues from the N-linked oligosaccharide had little effect on its utilization as a substrate for glucosidase I. The enzyme had a subunit molecular weight of 97 kDa on SDS gels and this was shifted to 94 kDa after treatment with Endo H or Endo F, suggesting that glucosidase I is an N-glycoprotein having one oligomannose-type oligosaccharide. Amino acid sequences of this enzyme showed considerable identity to the enzyme cloned from a human hippocampus cDNA library. The enzyme was inhibited by castanospermine, deoxynojirimycin, MDL, and trehazolin, but not by australine or kifunensine. On the other hand, the other processing glucosidase, glucosidase II, is sensitive to inhibition by australine, but not by trehazolin. Thus, these two inhibitors are useful to distinguish glucosidase I from glucosidase II. The mung bean g...Continue Reading

Citations

Apr 8, 2011·Molecular Biology of the Cell·Ivan D StiglianoCecilia D'Alessio
Sep 11, 2009·PloS One·Flávia Borges MuryMarilvia Dansa-Petretski
Feb 10, 2009·Phytochemistry·Renaud LéonardFriedrich Altmann
Sep 24, 2015·Plant Science : an International Journal of Experimental Plant Biology·Nausicaä Lannoo, Els J M Van Damme
Mar 12, 2004·International Journal for Parasitology·José C Bravo-TorresEverardo López-Romero
Apr 2, 2010·Antonie van Leeuwenhoek·María D Frade-PérezHéctor M Mora-Montes
Dec 19, 2003·Protein Expression and Purification·Amirreza Faridmoayer, Christine H Scaman

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