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  • Title: In vitro hydrolysis of oligomannose-type sugar chains by an alpha-1,2-mannosidase from microsomes of developing castor bean cotyledons.
    Author: Kimura Y, Yamaguchi O, Suehisa H, Takagi S.
    Journal: Biochim Biophys Acta; 1991 Sep 02; 1075(1):6-11. PubMed ID: 1832562.
    Abstract:
    An alpha-1,2-mannosidase involved in the processing of N-linked oligosaccharides was prepared from the microsomal fraction of developing castor bean cotyledons. The processing alpha-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-alpha-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 alpha-mannosidase revealed that specific intermediates were formed during conversion of Man9GlcNAc2-PA to Man5GlcNAc2-PA.
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