In vitro hydrolysis of oligomannose-type sugar chains by an α-1,2-mannosidase from microsomes of developing castor bean cotyledons

Kimura Yoshinobu Kimura, Yamaguchi Osamu Yamaguchi, Suehisa Hiroshi Suehisa, Takagi Shigeaki Takagi

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

An α-1,2-mannosidase involved in the processing of N-linked oligosaccharides was prepared from the microsomal fraction of developing castor bean cotyledons. The processing α-mannosidase was solubilized with 1.0% Triton X-100 and purified by ion-exchange chromatography followed by two gel filtration steps. The enzyme obtained could convert Man9GlcNAc2-PA to Man5GlcNAc2-PA, but this enzyme was inactive with Man5GlcNAc2-PA, Man4GlcNAc2-PA, and p-nitrophenyl-α-d-mannopyranoside. The enzyme was optimally active between pH 5.5-6.0. The processing mannosidase was inhibited by deoxymannojirimycin, EDTA, and Tris ions but not by swainsonine. Structural analyses of the mannose-trimming intermediates produced by the α-mannosidase revealed that specific intermediates were formed during conversion of Man9GlcNAc2-PA to Man5GlcNAc2-PA.

Original languageEnglish
Pages (from-to)6-11
Number of pages6
JournalBBA - General Subjects
Volume1075
Issue number1
DOIs
Publication statusPublished - Sep 2 1991

Keywords

  • (R. communis)
  • Pyridyl amino derivative
  • Sugar chain processing
  • α-1,2-Mannosidase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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