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

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
JournalBiochimica et Biophysica Acta - General Subjects
Volume1075
Issue number1
DOIs
Publication statusPublished - Sep 2 1991

Fingerprint

Castor Bean
Mannosidases
Cotyledon
Microsomes
Sugars
Hydrolysis
Mannose
Enzymes
Processing
Swainsonine
Trimming
Ion Exchange Chromatography
Octoxynol
Chromatography
Oligosaccharides
Edetic Acid
Gel Chromatography
Ion exchange
Gels
Ions

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

In vitro hydrolysis of oligomannose-type sugar chains by an α-1,2-mannosidase from microsomes of developing castor bean cotyledons. / Kimura, Yoshinobu; Osamu Yamaguchi, Yamaguchi; Hiroshi Suehisa, Suehisa; Shigeaki Takagi, Takagi.

In: Biochimica et Biophysica Acta - General Subjects, Vol. 1075, No. 1, 02.09.1991, p. 6-11.

Research output: Contribution to journalArticle

@article{bb1b098c317147eb8afc244ab29c2cd0,
title = "In vitro hydrolysis of oligomannose-type sugar chains by an α-1,2-mannosidase from microsomes of developing castor bean cotyledons",
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.",
keywords = "(R. communis), Pyridyl amino derivative, Sugar chain processing, α-1,2-Mannosidase",
author = "Yoshinobu Kimura and {Osamu Yamaguchi}, Yamaguchi and {Hiroshi Suehisa}, Suehisa and {Shigeaki Takagi}, Takagi",
year = "1991",
month = "9",
day = "2",
doi = "10.1016/0304-4165(91)90067-Q",
language = "English",
volume = "1075",
pages = "6--11",
journal = "Biochimica et Biophysica Acta - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - In vitro hydrolysis of oligomannose-type sugar chains by an α-1,2-mannosidase from microsomes of developing castor bean cotyledons

AU - Kimura, Yoshinobu

AU - Osamu Yamaguchi, Yamaguchi

AU - Hiroshi Suehisa, Suehisa

AU - Shigeaki Takagi, Takagi

PY - 1991/9/2

Y1 - 1991/9/2

N2 - 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.

AB - 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.

KW - (R. communis)

KW - Pyridyl amino derivative

KW - Sugar chain processing

KW - α-1,2-Mannosidase

UR - http://www.scopus.com/inward/record.url?scp=0025883304&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025883304&partnerID=8YFLogxK

U2 - 10.1016/0304-4165(91)90067-Q

DO - 10.1016/0304-4165(91)90067-Q

M3 - Article

C2 - 1832562

AN - SCOPUS:0025883304

VL - 1075

SP - 6

EP - 11

JO - Biochimica et Biophysica Acta - General Subjects

JF - Biochimica et Biophysica Acta - General Subjects

SN - 0304-4165

IS - 1

ER -